In silico protein interaction screening uncovers DONSON’s role in replication initiation
Open accessAbstract
CDC45-MCM2-7-GINS (CMG) helicase assembly is the central event in eukaryotic replication initiation. In yeast, a multi-subunit “pre-loading complex” (pre-LC) accompanies GINS to chromatin-bound MCM2-7, leading to CMG formation. Here, we report that DONSON, a metazoan protein mutated in microcephalic primordial dwarfism, is required for CMG assembly in vertebrates. Using AlphaFold to screen for protein-protein interactions followed by experimental validation, we show that DONSON scaffolds a vertebrate pre-LC containing GINS, TOPBP1, and DNA pol ε. Our evidence suggests that DONSON docks the pre-LC onto MCM2-7, delivering GINS to its binding site in CMG. A patient-derived DONSON mutation compromises CMG assembly and recapitulates microcephalic dwarfism in mice. These results unify our understanding of eukaryotic replication initiation, implicate defective CMG assembly in microcephalic dwarfism, and illustrate how in silico protein-protein interaction screening accelerates mechanistic discovery.
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In proteome wide screens, SPOC readily identified STK19, USP37, and DONSON partners whose function we validated.
“The power of SPOC is illustrated by the fact that in proteome wide screens, it readily identified STK19, USP37, and DONSON partners whose function we validated23,54,56.”
From Predictomes, a classifier-curated database of AlphaFold-modeled protein-protein interactions (2025) · cites this paper as [23]
The Results section (“Ab initio prediction of protein function using AlphaFold-Multimer”; page unavailable) reports a proteome-wide DONSON interactor screen, and the Discussion says its predicted functional partners were experimentally validated. But the paper describes the method as AF-M, not SPOC, and says identifying CMG assembly as DONSON’s function from the proteome-wide screen was clearest after a second, structure-guided round of predictions. This source supports the DONSON example, not the STK19 or USP37 examples attributed to the other citations. (LLM, conf=0.84)
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Cites
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“…was transfected with two CRISPR plasmids targeting the C-terminal coding region of the DONSON gene (targets: 5 ′ -TTAGGCTTACTT- TGGTGTTC-3 ′ , 5 ′ -TTAGGCTTACTTTGATGTTC- 3 ′ ) and a donor plasmid encoding mAID-mClover and a hygromycin resistant marker following a published protocol ( 38 , 68 ).”
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“S4C), all DONSON residues except those interacting with POLE2 (65-72) were deleted.”
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“Rabbit polyclonal antibodies against the following proteins were used as primary antibodies for Western blotting: DONSON (1:5000, described above) MCM7 [1:12,000, (31)] MCM4 (1:4000, Bethyl #A300-193A, RRID: AB_162720) MCM3 (1:4000, SantaCruz (H-215) #sc-292857) CDC45 [1:20,000, (56)] GINS [1:5000, (54)] POLEcat [1:5,…”
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“Disordered DONSON residues (1-6, 26-154, 330-369) were deleted, leaving only the globular domain and GINS-binding peptide (residues 7-25).”
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“Rabbit polyclonal antibodies against the following proteins were used as primary antibodies for Western blotting: DONSON (1:5000, described above) MCM7 [1:12,000, (31)] MCM4 (1:4000, Bethyl #A300-193A, RRID: AB_162720) MCM3 (1:4000, SantaCruz (H-215) #sc-292857) CDC45 [1:20,000, (56)] GINS [1:5000, (54)] POLEcat [1:5,…”
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Mutations in DONSON disrupt replication fork stability and cause microcephalic dwarfism
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“S18A) and result in partial loss of function by reducing protein levels ( 23 ).”
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Automated unrestricted multigene recombineering for multiprotein complex production
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“S15] and POLA1 [1:5000, (59), used in all POLA1 blots except in Figs.”
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“We speculate that disengagement andclockwiserotation ofthetwo MCMs, as seen during CMG assembly in yeast ( 45 ), might enable DONSON dimer binding to both MCM3 molecules simultaneously (fig.”
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“To test whether mammalian DONSON is also required for replication initiation, DONSON-AID2 cells were synchronized in G1 using lovastatin ( 39 ) and released into S phase.”
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“S4C), all DONSON residues except those interacting with POLE2 (65-72) were deleted.”
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“6D”
Efficient Initiation of DNA Replication in Eukaryotes Requires Dpb11/TopBP1-GINS Interaction
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BackgroundInfluentialExtracts for Analysis of DNA Replication in a Nucleus-Free System.Preprint
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“As shown in table S2, TOPBP1, MCM3, POLE2, SLD5, and DONSON were among the 350 most confident DONSON interactors (sheet 2) but GO-term analysis did not identify DNA replication as a DONSON-associated function.”
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“Indeed,knock-downofMTBPorTRESLIN, which act upstream of DONSON, reduces origin firing and increases fork rates, but unlike DONSON, does not cause fork asymmetry ( 11 , 12 , 47 ).”
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“DONSON is essential for cell proliferation inmammals (24).”
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“DONSON ’ s role in CMG assembly provides a mechanistic explanation for DONSON mutations discovered in MGS patients ( 50 , 51 ).”
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Novel role of DONSON in CMG helicase assembly during vertebrate DNA replication initiation
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“…with structure predictions in different organisms (table S1), evidence for DONSON-dependent GINS and CDC45 recruitment to chromatin in nuclear assembly egg extracts ( 42 , 43 ), and data from worms ( 44 ), our evidence suggests that DONSON is generally required for CMG assembly in metazoans.”
BackgroundZhang, J., Bellani, M., James, R., Pokharel, D., Zhang, Y.-Q., Reynolds, J., McNee, G. S., Jackson, A., Stewart, G., & Seidman, M. (2020) · Nature Communications · doi:10.1038/s41467-020-17449-1 · Cited by 39 · see citing works
Self-citationhumpty dumpty is required for developmental DNA amplification and cell proliferation in Drosophila.
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“Phenotypic analysis in Drosophila suggested that DONSON plays a role in DNA replication ( 25 ).”
BackgroundThe expanding genetic and clinical landscape associated with Meier-Gorlin syndrome
Nielsen-Dandoroff, E., Ruegg, M. S. G., & Bicknell, L. (2023) · European Journal of Human Genetics · doi:10.1038/s41431-023-01359-z · Cited by 37 · see citing works
Kingsley, G., Skagia, A., Passaretti, P., Fernandez-Cuesta, C., Reynolds-Winczura, A., Koscielniak, K., & Gambus, A. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad694 · Cited by 36 · cited 2× · see citing works
“Disordered DONSON residues (1-6, 26-154, 330-369) were deleted, leaving only the globular domain and GINS-binding peptide (residues 7-25).”
BackgroundDDK regulates replication initiation by controlling the multiplicity of Cdc45-GINS binding to Mcm2-7
Jesús-Kim, L. D., Friedman, L., Lõoke, M., Ramsoomair, C., Gelles, J., & Bell, S. (2020) · bioRxiv · doi:10.7554/elife.65471 · Cited by 36 · cited 1×
“Additional analysis demonstrated that in both M440T/M440T mESCs and mouse embryonic fibroblasts (MEFs), interorigin distance was substantially increased (Fig.”
BackgroundDNA replication of mitotic chromatin in Xenopus egg extracts
Prokhorova, T. A., Mowrer, K., Gilbert, C. H., & Walter, J. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2336104100 · Cited by 35 · cited 2× · see citing works
“Disordered DONSON residues (1-6, 26-154, 330-369) were deleted, leaving only the globular domain and GINS-binding peptide (residues 7-25).”
BackgroundSelf-citationTargeted Protein Depletion Using the Auxin‐Inducible Degron 2 (AID2) System
Saito, Y., & Kanemaki, M. T. (2021) · Current Protocols · doi:10.1002/cpz1.219 · Cited by 33 · cited 1× · see citing works
“…was transfected with two CRISPR plasmids targeting the C-terminal coding region of the DONSON gene (targets: 5 ′ -TTAGGCTTACTT- TGGTGTTC-3 ′ , 5 ′ -TTAGGCTTACTTTGATGTTC- 3 ′ ) and a donor plasmid encoding mAID-mClover and a hygromycin resistant marker following a published protocol ( 38 , 68 ).”
MethodSelf-citationPhosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1
Day, M., Oliver, A. W., & Pearl, L. H. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103232 · Cited by 32 · cited 1× · see citing works
“3E), consistent with the fact that the essential TOPBP1 BRCT domain that contacts DONSON (BRCT3) is not predicted to bind phospho-peptides ( 37 ).”
BackgroundPRIM1 deficiency causes a distinctive primordial dwarfism syndromePreprint
Parry, D. A., Tamayo-Orrego, L., Carroll, P., Marsh, J., Greene, P., Murina, O., Uggenti, C., Leitch, A., Partnership, S., Káposzta, R., et al. (2020) · Genes & Development · doi:10.1101/gad.340190.120 · Cited by 29 · see citing works
Self-citationAnalysis of Replicating Yeast Chromosomes by DNA Combing.
Gallo, D., Wang, G., Yip, C. M., & Brown, G. W. (2016) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot085118 · Cited by 26 · cited 16×
“S4C), all DONSON residues except those interacting with POLE2 (65-72) were deleted.”
BackgroundMethodInfluentialKaraca, E., Posey, J. E., Bostwick, B. L., Liu, P., Gezdirici, A., Yeşil, G., Coban‐Akdemir, Z., Bayram, Y., Harms, F. L., Meinecke, P., et al. (2019) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61315 · Cited by 22 · cited 2× · see citing works
“Disordered DONSON residues (1-6, 26-154, 330-369) were deleted, leaving only the globular domain and GINS-binding peptide (residues 7-25).”
BackgroundThe non-catalytic role of DNA polymerase epsilon in replication initiation in human cells
Vipat, S., Gupta, D., Jonchhe, S., Anderspuk, H., Rothenberg, E., & Moiseeva, T. N. (2022) · Nature Communications · doi:10.1038/s41467-022-34911-4 · Cited by 21 · cited 4× · see citing works
“4, A and B), consistent with previous studiesshowingCMGformationinPol e -deficient egg extracts and human cells ( 19 , 20 ).”
BackgroundMethodResultInfluentialSaito, Y., Santosa, V., Ishiguro, K.-I., & Kanemaki, M. T. (2022) · bioRxiv · doi:10.1101/2022.02.08.479529 · Cited by 15 · cited 1×
“All cells were grown at 37°C and 5% CO”
BackgroundSelf-citationSaito, Y., Santosa, V., Ishiguro, K.-I., & Kanemaki, M. T. (2022) · eLife · doi:10.7554/elife.77393 · Cited by 14 · see citing works
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Accurate structure prediction of biomolecular interactions with AlphaFold 3
Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861 · see citing works
Empowering Biomedical Discovery with AI AgentsPreprint
Gao, S., Fang, A., Huang, Y.-P., Giunchiglia, V., Noori, A., Schwarz, J., Ektefaie, Y., Kondic, J., & Zitnik, M. (2024) · Cell · doi:10.48550/arxiv.2404.02831 · Cited by 424 · see citing works
“For example, a study employed AlphaFold-Multimer to predict interactions of DONSON, a protein with limited understanding, leading to a hypothesis about its functions [79].”
Empowering biomedical discovery with AI agents
Gao, S., Fang, A., Huang, Y., Giunchiglia, V., Noori, A., Schwarz, J. R., Ektefaie, Y., Kondic, J., & Zitnik, M. (2024) · Cell · doi:10.1016/j.cell.2024.09.022 · Cited by 315 · see citing works
Discovery and significance of protein-protein interactions in health and disease
Greenblatt, J. F., Alberts, B., & Krogan, N. J. (2024) · Cell · doi:10.1016/j.cell.2024.10.038 · Cited by 171 · see citing works
Multiscale photocatalytic proximity labeling reveals cell surface neighbors on and between cells
Lin, Z., Schaefer, K., Lui, I., Yao, Z. W., Fossati, A., Swaney, D. L., Palar, A., Šali, A., & Wells, J. A. (2024) · Science · doi:10.1126/science.adl5763 · Cited by 155 · see citing works
“To provide a structural level of analysis, we turned to AlphaFold-Multimer, an extension of AlphaFold developed over the past few years that uses artificial intelligence to generate plausible models of binary protein complexes ( 25 , 56 , 57 ).”
BackgroundMethodPredictomes: A classifier-curated database of AlphaFold-modeled protein-protein interactions
(2024) · doi:10.1101/2024.04.09.588596 · Cited by 121 · see citing works
“We previously used in silico screening with AF-M to uncover how the protein DONSON promotes replication initiation 24 .”
MethodSelf-citationPredictomes, a classifier-curated database of AlphaFold-modeled protein-protein interactions
Schmid, E. W., & Walter, J. C. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.034 · Cited by 120 · see citing works
“Although this metric was useful in scoring a small-scale in silico screen, its performance was poor in a proteome-wide screen 33 .”
InfluentialSelf-citationFrom interaction networks to interfaces, scanning intrinsically disordered regions using AlphaFold2
Bret, H., Gao, J., Zea, D. J., Andreani, J., & Guerois, R. (2024) · Nature Communications · doi:10.1038/s41467-023-44288-7 · Cited by 103 · see citing works
Structure and dynamics in drug discovery
Wei, H., & McCammon, J. A. (2024) · npj Drug Discovery. · doi:10.1038/s44386-024-00001-2 · Cited by 94 · see citing works
AlphaFold two years on: Validation and impact
Kovalevskiy, O. V., Mateos-Garcia, J. C., & Tunyasuvunakool, K. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315002121 · Cited by 81 · see citing works
“To put this in context, the median rmsd for another PDB structure of the same pro - tein crystallized in a different space group would be 0.6 Å. Confidence scores were predictive of the level of agreement with deposited models, highlighting the importance of refer - ring to these when interpreting…”
InfluentialFrom intention to implementation: automating biomedical research via LLMs
Luo, Y., Shi, L., Li, Y., Zhuang, A., Gong, Y., Liu, L., & Chen, L. (2025) · Science China Information Sciences · doi:10.1007/s11432-024-4485-0 · Cited by 56 · see citing works
“Finally, the programming module extracts a sequence of dry lab experiment tasks from the protocol and generates accurate and executable codes for these tasks.”
Benchmarking all-atom biomolecular structure prediction with FoldBench
Xu, S. Y., Feng, Q., Qiao, L., Wu, H., Shen, T., Cheng, Y., Zheng, S., & Sun, S. (2025) · Nature Communications · doi:10.1038/s41467-025-67127-3 · Cited by 64 · see citing works
From Intention To Implementation: Automating Biomedical Research via LLMs
Luo, Y., Shi, L., Li, Y., Zhuang, A., Gong, Y., Liu, L., & Lin, C. (2024) · arXiv · doi:10.48550/arxiv.2412.09429 · Cited by 53
“Finally, the programming module extracts a sequence of dry lab experiment tasks from the protocol and generates accurate and executable codes for these tasks.”
STK19 positions TFIIH for cell-free transcription-coupled DNA repair
Mevissen, T. E. T., Kümmecke, M., Schmid, E. W., Farnung, L., & Walter, J. C. (2024) · Cell · doi:10.1016/j.cell.2024.10.020 · Cited by 50 · see citing works
Self-citationSTK19 positions TFIIH for cell-free transcription-coupled DNA repair
Mevissen, T. E. T., Kümmecke, M., Schmid, E. W., Farnung, L., & Walter, J. C. (2024) · doi:10.1101/2024.07.22.604623 · Cited by 50 · see citing works
“27,41 Briefly, confident interchain residue contacts were extracted from structures by identifying proximal residues (distance <5 Å) where both residues have pLDDT values >50 and PAE score 15 Å.”
Self-citationThe structural mechanism of dimeric DONSON in replicative helicase activation
Cvetkovic, M. A., Passaretti, P., Butryn, A., Reynolds-Winczura, A., Kingsley, G., Skagia, A., Fernandez-Cuesta, C., Poovathumkadavil, D., George, R., Chauhan, A. S., et al. (2023) · Molecules and Cells · doi:10.1016/j.molcel.2023.09.029 · Cited by 41 · see citing works
Yadav, A. K., & Polasek-Sedlackova, H. (2024) · Communications Biology · doi:10.1038/s42003-024-05855-w · Cited by 27 · see citing works
Xia, Y., Sonneville, R., Jenkyn-Bedford, M., Ji, L., Alabert, C., Hong, Y., Yeeles, J. T. P., & Labib, K. P. M. (2023) · Science · doi:10.1126/science.adi4932 · Cited by 41 · see citing works
“This suggests an evolutionarily conserved role for metazoan DONSON orthologs during DNA replication initiation, consistentwith recentdata forXenopusDONSON (53, 54).”
Emerging frontiers in protein structure prediction following the AlphaFold revolution
Rennie, M. L., & Oliver, M. R. (2025) · Journal of The Royal Society Interface · doi:10.1098/rsif.2024.0886 · Cited by 27 · see citing works
DONSON is required for CMG helicase assembly in the mammalian cell cycle
Evrin, C., Álvarez, V., Ainsworth, J., Fujisawa, R., Alabert, C., & Labib, K. P. M. (2023) · EMBO Reports · doi:10.15252/embr.202357677 · Cited by 24 · see citing works
Progress of AI-Driven Drug–Target Interaction Prediction and Lead Optimization
Wang, Q., Sun, B., Yi, Y., Velkov, T., Shen, J., Dai, C., & Jiang, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262010037 · Cited by 32 · see citing works
Machine learning to predict de novo protein–protein interactions
Gaínza, P., Bunker, R. D., Townson, S. A., & Castle, J. C. (2025) · Trends in biotechnology · doi:10.1016/j.tibtech.2025.04.013 · Cited by 25 · see citing works
Recent progress and future challenges in structure-based protein-protein interaction prediction
Yuan, R., Zhang, J., Zhou, J., & Cong, Q. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.04.003 · Cited by 20 · see citing works
“147 Yu et al. discovered that Mrc1/CLASPIN, a replication fork protection complex component, might interact with H3-H4 tetramer based on AFM predictions.”
Bias in, bias out – AlphaFold-Multimer and the structural complexity of protein interfaces
Strom, J. M., & Luck, K. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103002 · Cited by 22 · see citing works
Nasheuer, H., Meaney, A. M., Hulshoff, T., Thiele, I., & Onwubiko, N. O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25010588 · Cited by 21 · see citing works
Combinatorial mapping of E3 ubiquitin ligases to their target substrates
Suiter, C. C., Calderon, D., Lee, D. S., Chiu, M., Jain, S., Chardon, F. M., Lee, C., Daza, R. M., Trapnell, C., Zheng, N., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.016 · Cited by 21 · see citing works
“False positives could arise from non-specific effects, e.g., off-target events or cellular responses induced by Cas9-induced DSBs. 49”
Wells, J. N., Leber, V., Edwardes, L. V., Allyjaun, S., Peach, M., Tomkins, J., Kefala-Stavridi, A., Faull, S. V., Aramayo, R., Pestana, C. M., et al. (2024) · bioRxiv · doi:10.1038/s41467-024-55772-z · Cited by 15 · see citing works
Single-Molecule Imaging Reveals the Mechanism of Bidirectional Replication Initiation in Metazoa
Terui, R., Berger, S. E., Sambel, L. A., Song, D., & Chistol, G. (2024) · bioRxiv · doi:10.1101/2024.03.28.587265 · Cited by 15
“A similar model was recently proposed for metazoa, with the putative pre-LC consisting of either TopBP1(cid:129)DONSON(cid:129)GINS(cid:129)Pol ε or DONSON(cid:129)GINS(cid:129)Cdc45(cid:129)Pol ε 16,17 .”
Self-citationCombination of AID2 and BromoTag expands the utility of degron-based protein knockdowns
Hatoyama, Y., Islam, M., Bond, A., Hayashi, K.-I., Ciulli, A., & Kanemaki, M. T. (2024) · bioRxiv · doi:10.1038/s44319-024-00224-4 · Cited by 15 · see citing works
“Because our group is interested in DNA replication, we applied AID2 to control the expression of essential replication factors in human colorectal cancer HCT116 cells by biallelically tagging the endogenous target genes using CRISPR-Cas9 (Lim et al, 2023; Liu et al, 2023; Saito et al, 2022).”
Self-citationA conserved PIWI silencing complex detects piRNA-target engagement
De, D., Sarkar, S., Gebert, L. F., Wiryaman, T., Anzelon, T. A., & MacRae, I. J. (2025) · Molecules and Cells · doi:10.1016/j.molcel.2025.08.010 · Cited by 14 · see citing works
Assembly and activation of replicative helicases at origin DNA for replication initiation.
Zhang, Q., Lam, W.-H., & Zhai, Y. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102876 · Cited by 14
RECQL4 is not critical for firing of human DNA replication origins
Padayachy, L., Ntallis, S. G., & Halazonetis, T. D. (2024) · Scientific Reports · doi:10.1038/s41598-024-58404-0 · Cited by 14 · see citing works
TopBP1 utilises a bipartite GINS binding mode to support genome replication
Day, M., Tetik, B., Parlak, M., Almeida-Hernández, Y., Räschle, M., Kaschani, F., Siegert, H., Marko, A., Sanchez-Garcia, E., Kaiser, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45946-0 · Cited by 14 · see citing works
Starting DNA Synthesis: Initiation Processes during the Replication of Chromosomal DNA in Humans
Nasheuer, H., & Meaney, A. M. (2024) · Genes · doi:10.3390/genes15030360 · Cited by 18 · see citing works
Bilirubin Targeting WNK1 to Alleviate NLRP3‐Mediated Neuroinflammation
Mao, L., Lu, J., Yang, Q., Liu, Z.-Q., Wu, C., Ke, B., Su, K., Yuan, H., Cui, Y., Wang, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202407349 · Cited by 9 · see citing works
You, Z., & Masai, H. (2024) · Biology · doi:10.3390/biology13080629 · Cited by 11
“During CMG helicase assembly, DONSON, existing as a dimer, interacts with the BRCT3 domain of TopBP1 and is essential for placing the GINS complex onto the MCM2–7 helicase via its interactions with the AAA+ domain of MCM3 and the Sld5 subunit of GINS [116–118] (Figure 1C).”
BackgroundInfluentialMulti-scale photocatalytic proximity labeling reveals cell surface neighbors on and between cellsPreprint
Lin, Z., Schaefer, K., Lui, I., Yao, Z., Fossati, A., Swaney, D., Palar, A., Šali, A., & Wells, J. A. (2023) · bioRxiv · doi:10.1101/2023.10.28.564055 · Cited by 11 · see citing works
“Additional criteria can be applied including buried solvent accessible surface area (BSASA) ≥ 500Å 2 ( 55, 56 ), predicted local distance difference test (pLDDT)>50 for the interface residues and minimum predicted alignment error (PAE) 15 Å as described previously ( 52 ).”
BackgroundMethodSingle-Molecule Imaging Reveals the Mechanism of Bidirectional Replication Initiation in Metazoa
Terui, R., Berger, S. E., Sambel, L. A., Song, D., & Chistol, G. (2024) · Cell · doi:10.1016/j.cell.2024.05.024 · Cited by 10 · see citing works
Self-citationApproaches for accelerating microbial gene function discovery using artificial intelligence
Palsson, B. Ø., Lee, S. Y., & Kim, G. B. (2026) · Nature Microbiology · doi:10.1038/s41564-025-02214-1 · Cited by 7 · see citing works
Structural basis of Fanconi anemia pathway activation by FANCM
Bythell-Douglas, R., van Twest, S., Abbouche, L., Dunn, E., Coulthard, R., Briggs, D., Murphy, V. J., Zhang, X.-X., Tan, W., Henrikus, S. S., et al. (2025) · EMBO Journal · doi:10.1038/s44318-025-00468-3 · Cited by 9
“Through a combination of predictive modeling (using “ Predictomes ” (Lim et al, 2023)), and biochemical analysis, we identi fi ed FANCF as FANCM ’ s direct binding partner in the FA core complex (Fig.”
A tale of two strands: Decoding chromatin replication through strand-specific sequencing
Li, Z., & Zhang, Z. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.10.035 · Cited by 12 · see citing works
AlphaFold2 Predicts Whether Proteins Interact Amidst Confounding Structural Compatibility
Martin, J. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01805 · Cited by 19 · see citing works
Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines
Lewis, J. S., van Oijen, A. V., & Spenkelink, L. M. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00436 · Cited by 9 · see citing works
AlphaFold 3 Fails to Predict D-peptide Chirality, Fold, and Binding Pose in Heterochiral ComplexesPreprint
Childs, H., Zhou, P., & Donald, B. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.14.643307 · Cited by 16 · see citing works
Mischley, V., Maier, J., Chen, J., & Karanicolas, J. (2026) · eLife · doi:10.7554/elife.98179 · Cited by 8 · see citing works
“…– which range from predicting protein quaternary structures to defining biological functions of peptides and intrinsically disordered regions ( Lim et al., 2023 ; Bret et al., 2024 ; Danneskiold-Samsøe et al., 2023 ; Marciano et al., 2022 ; Martin, 2024 ; Teufel et al., 2023 ; Pogozheva et…”
In silico discovery of nanobody binders to a G-protein coupled receptor using AlphaFold-Multimer
Harvey, E. P., Smith, J. S., Hurley, J. D., Granados, A. J., Schmid, E. W., Liang-Lin, J. G., Zhang, H., Meara, E. M., Wren, E. K., Paul, S., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72093-5 · Cited by 7 · see citing works
“…manner, we utilized a modi fi ed AF-M ColabFold script optimized for faster prediction speed and decreased memory storage requirements 8,16,17 , and we generated structural predictions of these curated nanobody-antigen pairs to investigate which outputs, if any, were predictive of…”
Self-citationde Oliveira, R. C., Cavalcante, G. C., & Soares-Souza, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312585 · Cited by 7 · see citing works
A common mechanism for recruiting the Rrm3 and RTEL1 accessory helicases to the eukaryotic replisome
Olson, O., Pelliciari, S., Heron, E. D., & Deegan, T. (2024) · EMBO Journal · doi:10.1038/s44318-024-00168-4 · Cited by 6 · see citing works
“6, site 3) overlap with binding sites for POLA2 (Jones et al, 2023) and DONSON (Cvetkovic et al, 2023; Lim et al, 2023; Xia et al, 2023), respectively.”
USP37 prevents premature disassembly of stressed replisomes by TRAIP
Kochenova, O. V., D’Alessandro, G., Pilger, D., Schmid, E., Richards, S. L., Garcia, M. R., Jhujh, S. S., Voigt, A., Gupta, V., Carnie, C. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60139-z · Cited by 6 · see citing works
Self-citationGuo, K., Xu, S., Sun, C., Yan, W., Yan, J., Yu, H., Wang, C. Q., Xu, W., Li, J., Bi, Z., et al. (2026) · Materials Today · doi:10.1016/j.mattod.2026.103371 · Cited by 5 · see citing works
A CDK1 phospho-switch reprograms TRAIP to unload replisomes in mitosis
Can, G., Shyian, M., Krishnamoorthy, A., Ahmed, S., Lim, Y., Wu, A., Pavani, R., Zaher, M. S., Nussenzweig, A., Räschle, M., et al. (2026) · Science · doi:10.1126/science.aeh1834 · Cited by 13 · see citing works
Self-citationHierarchical small molecule inhibition of MYST acetyltransferases
Chen, X., Castroverde, A., Perez, M., Holewinski, R., Suazo, K. F., Karki, R., Andresson, T., Garcia, B. A., & Meier, J. L. (2026) · Nature Communications · doi:10.1038/s41467-026-70574-1 · Cited by 5
“To better understand the ability of FOXK2 to interact with MYST complexes, we performed an in silico interaction screen using AlphaPulldown 33,34 .”
MCM5 UFMylation regulates replication origin firing and fork progression
Li, Z., Wu, X., Liu, L., Rao, S., Liao, Y., Liu, M., Peng, B., Zhang, Q., Xia, Y., Zhai, Y., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00562-6 · Cited by 7 · see citing works
“…is an essential component for loading GINS onto MCM hexamers (Cvetkovic et al, 2023; Evrin et al, 2023; Kingsley et al, 2023; Xia et al, 2023; Lim et al, 2023; Hashimoto et al, 2023; Terui et al, 2024), maintaining CMG helicase function during replication progression, and preventing…”
Viral RNA pUGylation Promotes Antiviral Immunity in C. elegans
Lowe, D. D., Shukla, A., & Kennedy, S. G. (2025) · bioRxiv · doi:10.1101/2025.07.09.663919 · Cited by 5
“…metrics to predict protein-protein interactions: (i) interface-predicted template modeling (ipTM) scores, which estimate interaction likelihood (44), and (ii) the number of independent structure predictions (out of five) that support the interaction, which indicates prediction robustness (45).”
In silico screening identifies SHPRH as a novel nucleosome acidic patch interactorPreprint
James, A. M., Schmid, E. W., Walter, J. C., & Farnung, L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.26.600687 · Cited by 5 · see citing works
Self-citationDONSON: Slding in 2 the limelight.
Stewart, G. S. (2023) · DNA Repair · doi:10.1016/j.dnarep.2023.103616 · Cited by 5
Structure of the pre-initiation complex explains CMGE biogenesis
Pühringer, T., Canal, B., Palm, G., Butryn, A., Couves, E. C., Willhoft, O., Lewis, J. S., Diffley, J., & Costa, A. (2026) · bioRxiv · doi:10.1038/s41586-026-10657-7 · Cited by 4 · see citing works
Structure and function of IWS1 in transcription elongation
Syau, D., Steinruecke, F., Roth, S., Schmid, E., Adelman, K., Walter, J. C., & Farnung, L. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag357 · Cited by 5 · see citing works
“…value above 0.5 is generally considered confident. pDockQ [ 43 ] estimates of interface accuracy scores were calculated independently of the contact analysis described above using code that was adapted from the original implementation [ 49 ]. pDockQ values above 0.23 are considered confident.”
InfluentialSelf-citationRare genetic diseases associated with G-quadruplex-induced replication stress
Herr, L. M., Mukhopadhyay, S., Anderson, O. M., Couch, T. H., Jones, C. M., Brosh, R. M., & Rossi, M. S. (2026) · Communications Biology · doi:10.1038/s42003-026-09966-4 · Cited by 3 · see citing works
Forecasting SARS-CoV-2 spike protein evolution from small data by deep learning and regression
King, S. B., Chen, X. E., Ng, S. W. S., Rostin, K., Hahn, S. V., Roberts, T., Schwab, J. C., Sekhon, P., Kagieva, M., Reilly, T., et al. (2024) · Frontiers in Systems Biology · doi:10.3389/fsysb.2024.1284668 · Cited by 7 · see citing works
USP37 prevents premature disassembly of stressed replisomes by TRAIP
Kochenova, O. V., D’Alessandro, G., Pilger, D., Schmid, E., Richards, S. L., Garcia, M. R., Jhujh, S. S., Voigt, A., Gupta, V., Carnie, C. J., et al. (2024) · doi:10.1101/2024.09.03.611025 · Cited by 3 · see citing works
“50 ).”
Self-citationThe transformative power of structural predictions with AI in plant science
Lyu, J., & van der Hoorn, R. V. D. (2026) · The Plant Journal · doi:10.1111/tpj.70807 · Cited by 3
“For example, AlphaFold-Multimer has been used to identify interactors of proteins of interests across different systems, with predicted models subsequently informing experimentally testable hypotheses (Homma et al., 2023; Lim et al., 2023; Poitras et al., 2023).”
Ramírez-Guadiana, F. H., Brogan, A. P., Yu, Y.-C., Midonet, C., Sher, J. W., Schmid, E. W., Roney, I. J., & Rudner, D. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003521 · Cited by 3 · see citing works
“Five independent models were generated for each prediction and the confidence metrics were analyzed using a published pipeline [58].”
Self-citationLuo, C., Wang, L., Wu, Y.-Q., Cai, J., Peng, B., Chen, J., Yu, F., & Wu, D.-S. (2025) · Plant, Cell and Environment · doi:10.1111/pce.70219 · Cited by 3 · see citing works
Matsuhashi, K., Ito, K. K., Nagai, K., Sanada, A., Watanabe, K., Takumi, K., Toyoda, A., Fukuyama, M., Yamamoto, S., Chinen, T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63002-3 · Cited by 3 · see citing works
“Recent studies revealed that the formation of the CMG helicase is mediated by Downstream Neighbor of SON (DONSON), which delivers accessory proteins to the MCM motor 13 – 16 .”
Najafi, N. N., Karbassian, R., Hajihassani, H., & Irani, M. A. (2025) · Journal of Molecular Modeling · doi:10.1007/s00894-025-06392-x · Cited by 3 · see citing works
Predicting Protein Function in the AI and Big Data Era
Percudani, R., & Rito, C. D. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00186 · Cited by 3 · see citing works
The non-catalytic ε DNA polymerase subunit is an NPF motif recognition protein
Keskitalo, S., Zámbó, B., Tuhkala, A., Salokas, K., Turunen, T., Deutsch, N., Davey, N., Dosztányi, Z., Varjosalo, M., & Gógl, G. (2025) · bioRxiv · doi:10.1101/2025.03.17.643635 · Cited by 3 · see citing works
“…in parallel to our investigation, two reporting that the non-catalytic ε DNA polymerase subunit (POLE2) can interact with NPF motifs found in Protein downstream neighbor of Son (DONSON) 25,26 , and two reporting an interaction between POLE2 and the transcription termination factor 2 (TTF2) 27,28 .”
How similar are the molecular mechanisms of yeast and metazoan genome replication initiation?
Palm, G., & Costa, A. (2025) · Biochemical Society Transactions · doi:10.1042/bst20220917 · Cited by 3 · see citing works
S-CDK-regulated bipartite interaction of Mcm10 with MCM is essential for DNA replication
Wang, X., Liu, L., Chen, M., Quan, Y., Zhang, J.-X., Lou, H., Xia, Y.-S., Chen, H., & Hou, W.-Y. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1420033 · Cited by 3
A second hotspot for pathogenic exon-skipping variants in CDC45
Schoch, K., Ruegg, M. S. G., Fellows, B. J., Cao, J., Uhrig, S., Einsele-Scholz, S., Biskup, S., Hawarden, S. R. A., Salpietro, V., Capra, V., et al. (2024) · European Journal of Human Genetics · doi:10.1038/s41431-024-01583-1 · Cited by 3 · see citing works
“The intricacies of this pathway are still being uncovered, such as the recent multiple descriptions reporting dynamic interactions linking DONSON, MCM helicase and GINS (and indirectly CDC45) as being necessary for preIC assembly and activity [3 – 5].”
BackgroundAmes, A., Seman, M., Larkin, A., Raiymbek, G., Chen, Z., Levashkevich, A., Kim, B., Biteen, J. S., & Ragunathan, K. (2024) · Nature Communications · doi:10.1038/s41467-024-50538-z · Cited by 5 · see citing works
“Swi6 proteins were diluted to 100 nM in 20mM HEPES pH 7.5, 100mM KCl immediately before taking measurements.”
InfluentialA broadly conserved gram-positive lipoprotein regulates cell elongation
Brogan, A. P., Schmid, E. W., & Rudner, D. (2026) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2610431123 · Cited by 2 · see citing works
“To analyze the results of the pairwise screen, we utilized a published analysis pipeline (34).”
Self-citationMcm10 braces converging replicative helicases to pull apart origin DNAPreprint
Palm, G., Butryn, A., Canal, B., Pühringer, T., Gross, M. H., Diffley, J., & Costa, A. (2026) · bioRxiv · doi:10.64898/2026.05.15.725099 · Cited by 2 · see citing works
Hunker, O., & Bleichert, F. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00628-5 · Cited by 1 · see citing works
“…identi fi ed DONSON as a crucial missing link in the establishment of bidirectional replication through a protein – protein interaction screen (Lim et al, 2023), and integrated AlphaFold predictions with cryo-EM to achieve an unprecedented, near-complete model of the nuclear pore complex…”
InfluentialViral RNA pUGylation promotes antiviral immunity in C. elegans
Lowe, D. D., Shukla, A., & Kennedy, S. G. (2025) · Journal of Virology · doi:10.1128/jvi.01169-25 · Cited by 2 · see citing works
The dramatic impact of the PER-DBT interaction on circadian timekeeping and temperature compensationPreprint
Petersen, E. N., Keefer, E., Ludewig, H., Sullivan, C., Kern, D., & Rosbash, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.01.636007 · Cited by 1 · see citing works
“…protein structure and protein-protein interactions 44,45 and has even been used to screen for novel interactors in large protein complexes 46–48 ; AlphaFold generated the first high confidence atomic model of the CK1/DBT-PER interaction, some of which we successfully tested…”
Structure and function of IWS1 in transcription elongation
Syau, D., Steinruecke, F., Roth, S., Schmid, E. W., Adelman, K., Walter, J. C., & Farnung, L. (2025) · bioRxiv · doi:10.1101/2025.08.28.672863 · Cited by 2
Self-citationKoit, S., Tamberg, N., Reinapae, A., Peil, L., Kristjuhan, A., & Ilves, I. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108408 · Cited by 2 · see citing works
Zhang, Z.-Q., & Elledge, S. (2024) · bioRxiv · doi:10.1101/2024.10.20.619305 · Cited by 2 · see citing works
Pioneer factors for DNA replication initiation in metazoans
Wang, Y., & Liang, J. (2024) · Bioessays · doi:10.1002/bies.202400002 · Cited by 2
Establishing a biochemical understanding of the initiation of chromosome replication in bacteria
Stillman, B. (2024) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2400667121 · Cited by 2
The Response of the Replication Apparatus to Leading Template Strand Blocks
Bellani, M., Shaik, A., Majumdar, I., Ling, C., & Seidman, M. M. (2023) · Cells · doi:10.3390/cells12222607 · Cited by 2 · see citing works
Mitotic single-stranded DNA suppression by DDIAS.
Xue, Y., Rashed, F. B., Mao, D. Y. L., Abe, K., Lin, Z.-Y., Krastev, D., Setiaputra, D., Hoeg, L., Bonnet, C., Kumar, A., et al. (2026) · Molecules and Cells · doi:10.1016/j.molcel.2026.07.034 · Cited by 1 · see citing works
Spatial organization and dynamics of genome replication: from forks to foci
Pradhan, S. K., Arroyo, M., Pabba, M. K., Leonhardt, H., & Cardoso, M. C. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag550 · Cited by 1 · see citing works
“New developments using AI-based modeling of interactions with AlphaFold have paved the way for an in silico detailed analysis of the replisome organization and for the discovery of new replisome components [ 149 ].”
Bektash, A., Zhu, X.-X., Hatoyama, Y., Toyoda, A., & Kanemaki, M. T. (2026) · bioRxiv · doi:10.64898/2026.04.01.715782 · Cited by 1
“However, recent studies identified DONSON as fulfilling this role in vertebrate CMG assembly (Lim et al. 2023; Xia et al. 2023; Hashimoto et al. 2023) , prompting a reassessment of the role of RECQL4 in replication initiation.”
Self-citationMCM10 and SLD-2/RECQL4 jointly activate the CMG helicase during metazoan DNA replication initiation
Sonneville, R., Evrin, C., Wright, J. E., Huang, H., Xia, Y.-S., & Labib, K. (2026) · bioRxiv · doi:10.1038/s44318-026-00915-9 · Cited by 1
An updated view on lagging strand DNA replication: implications for the replication stress response
Martín-Rufo, R., & Lecona, E. (2026) · Cell Cycle · doi:10.1080/15384101.2026.2646889 · Cited by 1 · see citing works
“Interestingly, the docking site for DONSON in the CMG overlaps with the interaction site for Pol α/Pri [17,37], as both of them contact the same region in MCM3 [17,40].”
Minute amounts of helicase-deficient truncated RECQL4 are sufficient for DNA replication
Buco, P., Castillo-Tandazo, W., Chalk, A., Pilcher, C., Holien, J. K., Heierhorst, J., Tan, T. Y., Koren, A., Smeets, M., & Walkley, C. R. (2026) · EMBO Reports · doi:10.1038/s44319-026-00727-2 · Cited by 1 · see citing works
“…essential yeast DNA replication factor Sld2, it has been proposed that a structurally unrelated protein DONSON has evolved to carry out the Sld2-like function during mammalian DNA replication (Cvetkovic et al, 2023; Evrin et al, 2023; Hashimoto et al, 2023; Kingsley et al, 2023; Lim et al, 2023).”
Gribkova, A. K., Armeev, G. A., Kirpichnikov, M. P., & Shaytan, A. К. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1489 · Cited by 3 · see citing works
“We envision that the development and application of AI-based structure prediction tools will facilitate chromatin research, particular in analysis of protein–protein interactions, which is already happening [ 102 , 103 ].”
The non-catalytic DNA polymerase ε subunit is an NPF motif recognition protein
Keskitalo, S., Zámbó, B., Pinar, D. M., Tuhkala, A., Salokas, K., Turunen, T., Deutsch, N., Davey, N., Dosztányi, Z., Varjosalo, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-67284-5 · Cited by 1 · see citing works
Dashora, V., Singh, A., Pandey, A., & Saha, S. (2025) · BMC Microbiology · doi:10.1186/s12866-025-04377-7
Walker, D. R., Fujimura, G., Vanegas, J. M., & Barbar, E. J. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1531793 · Cited by 1 · see citing works
Wu, K., & Pan, Z.-Q. (2025) · Molecules and Cells · doi:10.1016/j.molcel.2025.01.028 · Cited by 1 · see citing works
Meiotic recombination proteins in cancer.
Amodeo, V., Pettitt, S., Tutt, A., & Lord, C. (2026) · DNA Repair · doi:10.1016/j.dnarep.2026.103963
Li, Z., Shinohara, A., Xia, Y.-S., Xu, X.-Z., & Takeda, S. (2026) · Bioessays · doi:10.1002/bies.70185
DONSON links tumor-cell survival to MIF-associated macrophage remodeling in small cell lung cancer
Du, Q.-W., Li, R., Mei, T., Ma, S.-X., Wu, Y.-F., Li, P., Wang, L.-L., He, Z.-Y., & Wang, Q.-M. (2026) · Apoptosis · doi:10.1007/s10495-026-02441-9
Integrating structural and biological evidence to rerank ESMFold2 protein-protein interactionsPreprint
Xie, J., Li, M., Chai, Y., Ou, G., Li, W., & Guo, Z. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.16.751194
The predicted interactome of the human mitochondrial proteome
Swaminathan, A. B., Zulkifli, M., Guerra, R. M., Calabrese, S. M., Kalafatis, D. T., Pagliarini, D., & Gohil, V. M. (2026) · Nature Communications · doi:10.1038/s41467-026-77112-z
“AlthoughAFMwasoriginallydevelopedtopredictthestructureof multimeric protein complexes of known stoichiometry, a few recent studies have explored the potential of AFM to identify new protein-protein interactions 22 – 24 , 42 .”
Soeding, A., Willerding, L., Riemann, L., & Reuter, L. M. (2026) · Biological chemistry · doi:10.1515/hsz-2026-0167
“Alongside DONSON-dependent Cdc45-GINS recruitment and CMG assembly, this links limiting fi ring factors, MCM2-7 phosphorylation, and replication-timing establishment in a given cell population (Hashimoto et al. 2023; Lim et al. 2023).”
- Authors
- Lim, Y., Tamayo-Orrego, L., Schmid, E., Tarnauskaite, Z., Kochenova, O. V., Gruar, R., Muramatsu, S., Lynch, L., Schlie, A. V., Carroll, P. L., Chistol, G., Reijns, M. A. M., Kanemaki, M. T., Jackson, A. P., & Walter, J. C.
- Affiliations
- Harvard University (US)
- Institute of Genetics and Cancer (GB)
- MRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, Edinburgh, EH4 2XU, UK.
- Howard Hughes Medical Institute (US)
- National Institute of Genetics (JP)
- Stanford Medicine (US)
- Corresponding author
- Lim, Yang
- Tamayo-Orrego, Lukas
- Jackson, Andrew P.
- Walter, Johannes C.
- ORCID
- Venue
- Science
- Published
- 2023-09-22
- Volume
- 381
- Issue
- 6664
- Pages
- eadi3448-eadi3448
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC10801813
- OpenAlex
- W4385925982
- Cited by
- 112
- References
- 82
- Citations by year
- 2026: 29 · 2025: 37 · 2024: 39 · 2023: 7
- FWCI
- 9.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Science (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, cc-by)
- Funders
- National Science Foundation (2144481, CREST, 2140743, CAREER)
- Howard Hughes Medical Institute
- European Commission (HORIZON2020)
- National Institutes of Health
- Medical Research Council (MC_UU_00035/10)
- Japan Society for the Promotion of Science (21H04719, JP23H04925, CREST, JP21H0419)
- National Heart, Lung, and Blood Institute (R01HL098316)
- National Institute of General Medical Sciences (GM147060, T32GM007276, R35GM147060)
- Core Research for Evolutional Science and Technology (JPMJCR21E6)
- H2020 European Research Council (788093)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- DNA replication initiation, MCM2-7 complex, GINS, TopBP1, DNA polymerase epsilon, protein-protein interaction screening, AlphaFold
- MeSH terms
- Animals, Computer Simulation, DNA Replication, DNA-Binding Proteins, Dwarfism, Humans, Microcephaly, Nuclear Proteins, Saccharomyces cerevisiae, Xenopus laevis, Cell Cycle Proteins, Protein Interaction Mapping, Saccharomyces cerevisiae Proteins, Mice, Minichromosome Maintenance Proteins
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