A putative cap binding protein and the methyl phosphate capping enzyme Bin3/MePCE function in telomerase biogenesis
Open accessPreprint — published as 10.1038/s41467-022-28545-9 · Paper page
Abstract
Telomerase reverse transcriptase (TERT) and the noncoding telomerase RNA (TR) subunit constitute the core of telomerase. Additional subunits are required for ribonucleoprotein complex assembly and in some cases remain stably associated with the active holoenzyme. Pof8, a member of the LARP7 protein family is such a constitutive component of telomerase in fission yeast. Using affinity purification of Pof8, we have identified two previously uncharacterized proteins that form a complex with Pof8 and participate in telomerase biogenesis. Both proteins participate in ribonucleoprotein complex assembly and are required for wildtype telomerase activity and telomere length maintenance. One factor we named Thc1 ( T elomerase H oloenzyme C omponent 1) shares structural similarity with the nuclear cap binding complex and the poly-adenosine ribonuclease (PARN), the other is the ortholog of the methyl phosphate capping enzyme (Bin3/MePCE) in metazoans and was named Bmc1 ( B in3/ M eP C E 1) to reflect its evolutionary roots. Thc1 and Bmc1 function together with Pof8 in recognizing correctly folded telomerase RNA and promoting the recruitment of the Lsm2-8 complex and the catalytic subunit to assemble functional telomerase.
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Cites
Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2
Love, M. I., Huber, W., & Anders, S. (2014) · Genome Biology · doi:10.1186/s13059-014-0550-8 · Cited by 95,106 · see citing works
STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709 · see citing works
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Tabb, D. L., McDonald, W. H., & Yates, J. R. (2002) · Journal of Proteome Research · doi:10.1021/pr015504q · Cited by 1,369 · see citing works
Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe
Kim, D.-U., Hayles, J., Kim, D., Wood, V., Park, H.-O., Won, M., Yoo, H.-S., Duhig, T., Nam, M., Palmer, G., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1628 · Cited by 742 · see citing works
Telomeres: history, health, and hallmarks of aging
Chakravarti, D., LaBella, K. A., & DePinho, R. A. (2021) · Cell · doi:10.1016/j.cell.2020.12.028 · Cited by 637 · see citing works
pyGenomeTracks: reproducible plots for multivariate genomic datasets
Lopez‐Delisle, L., Rabbani, L., Wolff, J., Bhardwaj, V., Backofen, R., Grüning, B. A., Ramírez, F., & Manke, T. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa692 · Cited by 536 · see citing works
ProLuCID: An improved SEQUEST-like algorithm with enhanced sensitivity and specificity
Xu, T., Park, S. K., Venable, J. D., Wohlschlegel, J. A., Diedrich, J. K., Cociorva, D., Lu, B., Liao, L., Hewel, J., Han, X., et al. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.07.001 · Cited by 511 · see citing works
Fast and accurate automatic structure prediction with HHpred
Hildebrand, A., Remmert, M., Biegert, A., & Söding, J. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22499 · Cited by 469 · see citing works
Stuart, B. D., Choi, J., Zaidi, S., Xing, C., Holohan, B., Chen, R., Choi, M., Dharwadkar, P., Torres, F., Girod, C. E., et al. (2015) · Nature Genetics · doi:10.1038/ng.3278 · Cited by 469 · see citing works
Jerónimo, C., Forget, D., Bouchard, A., Li, Q., Chua, G., Poitras, C., Thérien, C., Bergeron, D., Bourassa, S., Greenblatt, J., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.027 · Cited by 444 · see citing works
Zhang, Y., Wen, Z., Washburn, M. P., & Florens, L. A. (2010) · Analytical Chemistry · doi:10.1021/ac9023999 · Cited by 386 · see citing works
Self-citationStefano, J. E. (1984) · Cell · doi:10.1016/0092-8674(84)90083-7 · Cited by 375 · see citing works
McDonald, W. H., Tabb, D. L., Sadygov, R. G., MacCoss, M. J., Venable, J. D., Graumann, J., Johnson, J. R., Cociorva, D., & Yates, J. R. (2004) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1603 · Cited by 345 · see citing works
Regulation of human telomerase in homeostasis and disease
Roake, C. M., & Artandi, S. E. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0234-z · Cited by 341 · see citing works
McDonald, W. H., Ohi, R., Miyamoto, D. T., Mitchison, T. J., & Yates, J. R. (2002) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(02)00563-8 · Cited by 304 · see citing works
Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
Seto, A., Zaug, A., Sobel, S. G., Wolin, S., & Cech, T. (1999) · Nature · doi:10.1038/43694 · Cited by 298 · see citing works
Two Modes of Survival of Fission Yeast Without Telomerase
Nakamura, T., Cooper, J. P., & Cech, T. R. (1998) · Science · doi:10.1126/science.282.5388.493 · Cited by 280 · see citing works
Proteomic Analysis by Multidimensional Protein Identification Technology
Florens, L. A., & Washburn, M. P. (2006) · Humana Press eBooks · doi:10.1385/1-59745-026-x:159 · Cited by 242 · see citing works
Self-citationTelomerase Mechanism of Telomere Synthesis
Wu, R. A., Upton, H. E., Vogan, J. M., & Collins, K. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045019 · Cited by 208 · see citing works
Poly(A)-specific ribonuclease deficiency impacts telomere biology and causes dyskeratosis congenita
Tummala, H., Walne, A. J., Collopy, L. C., Cardoso, S. R., de la Fuente, J., Lawson, S., Powell, J., Cooper, N. S., Foster, A. C., Mohammed, S. N., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78963 · Cited by 198 · see citing works
Lee, N. N., Chalamcharla, V. R., Reyes‐Turcu, F. E., Mehta, S. S., Zofall, M., Balachandran, V., Dhakshnamoorthy, J., Taneja, N., Yamanaka, S., Zhou, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.10.027 · Cited by 185 · see citing works
Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein
Stone, M. D., Mihalusova, M., O’Connor, C. M., Prathapam, R., Collins, K., & Zhuang, X. (2007) · Nature · doi:10.1038/nature05600 · Cited by 184 · see citing works
Poly(A)-specific ribonuclease (PARN) mediates 3′-end maturation of the telomerase RNA component
Moon, D. H., Segal, M., Boyraz, B., Guinan, E. C., Hofmann, I., Cahan, P., Tai, A., & Agarwal, S. (2015) · Nature Genetics · doi:10.1038/ng.3423 · Cited by 183 · see citing works
A genome-wide resource of cell cycle and cell shape genes of fission yeast
Hayles, J., Wood, V., Jeffery, L., Hoe, K., Kim, D.-U., Park, H.-O., Salas-Pino, S., Heichinger, C., & Nurse, P. (2013) · Open Biology · doi:10.1098/rsob.130053 · Cited by 171 · see citing works
Protection of Telomeres by the Ku Protein in Fission Yeast
Baumann, P., & Cech, T. R. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.10.3265 · Cited by 168 · see citing works
Self-citationTeplova, M., Yuan, Y.-R., Phan, A. T., Malinina, L. V., Ilin, S., Теплов, А. А., & Patel, D. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.10.027 · Cited by 158 · see citing works
Telomere-associated aging disorders
Opresko, P. L., & Shay, J. W. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.009 · Cited by 155 · see citing works
Human Telomerase RNA Processing and Quality Control
Tseng, C.-K., Wang, H.-F., Burns, A. M., Schroeder, M. R., Gaspari, M., & Baumann, P. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.075 · Cited by 148 · see citing works
Self-citationHoloenzyme proteins required for the physiological assembly and activity of telomerasePreprint
Witkin, K. L., & Collins, K. (2004) · Genes & Development · doi:10.1101/gad.1201704 · Cited by 143 · see citing works
The La and related RNA ‐binding proteins (LARPs): structures, functions, and evolving perspectives
Maraia, R. J., Mattijssen, S., Cruz‐Gallardo, I., & Conte, M. R. (2017) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1430 · Cited by 140 · see citing works
Xue, Y., Yang, Z., Chen, R., & Zhou, Q. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp977 · Cited by 124 · see citing works
TER1, the RNA subunit of fission yeast telomerase
Leonardi, J., Box, J. A., Bunch, J. T., & Baumann, P. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1343 · Cited by 123 · see citing works
Self-citationNguyen, D., St-Sauveur, V. G., Bergeron, D., Dupuis‐Sandoval, F., Scott, M. S., & Bachand, F. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.003 · Cited by 121 · see citing works
Identification and characterization of the Schizosaccharomyces pombe TER1 telomerase RNA
Webb, C. J., & Zakian, V. A. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1354 · Cited by 114 · see citing works
Singh, M., Wang, Z., Koo, B.-K., Patel, A., Cascio, D., Collins, K., & Feigon, J. F. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.018 · Cited by 99 · see citing works
Spliceosomal cleavage generates the 3′ end of telomerase RNA
Box, J. A., Bunch, J. T., Tang, W., & Baumann, P. (2008) · Nature · doi:10.1038/nature07584 · Cited by 99 · see citing works
Self-citationTelomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes
Tang, W., Kannan, R., Blanchette, M., & Baumann, P. (2012) · Nature · doi:10.1038/nature10924 · Cited by 96 · see citing works
Self-citationEuplotes telomerase contains an La motif protein produced by apparent translational frameshifting
Aigner, S., Lingner, J., Goodrich, K. J., Grosshans, C. A., Shevchenko, A., Mann, M., & Cech, T. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.6230 · Cited by 94 · see citing works
LARP7-Mediated U6 snRNA Modification Ensures Splicing Fidelity and Spermatogenesis in Mice
Wang, X., Li, Z., Yan, Y., Lin, P., Tang, W., Hasler, D., Meduri, R., Ye, L., Hua, M.-M., Qi, H.-T., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.002 · Cited by 65 · see citing works
Prathapam, R., Witkin, K. L., O'Connor, C. M., & Collins, K. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb900 · Cited by 64 · see citing works
Hasler, D., Meduri, R., Bąk, M., Lehmann, G. J., Heizinger, L., Wang, X., Li, Z.-T., Sement, F. M., Bruckmann, A., Dock‐Brégeon, A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.001 · Cited by 62 · see citing works
Ford, L. P., Shay, J. W., & Wright, W. E. (2001) · RNA · doi:10.1017/s1355838201010159 · Cited by 57 · see citing works
pDblet, a stable autonomously replicating shuttle vector for Schizosaccharomyces pombe
Brun, C., Dubey, D. D., & Huberman, J. A. (1995) · Gene · doi:10.1016/0378-1119(95)00497-t · Cited by 53 · see citing works
The Sm Complex Is Required for the Processing of Non-Coding RNAs by the Exosome
Coy, S., Volanakis, A., Shah, S., & Vasiljeva, L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065606 · Cited by 48 · see citing works
Gruber, A. R., Kilgus, C., Axel Mosig, A., Hofacker, I. L., Hennig, W., & Stadler, P. F. (2008) · Molecular Biology and Evolution · doi:10.1093/molbev/msn140 · Cited by 48 · see citing works
Improving Proteomics Mass Accuracy by Dynamic Offline Lock Mass
Zhang, Y., Wen, Z., Washburn, M. P., & Florens, L. A. (2011) · Analytical Chemistry · doi:10.1021/ac201867h · Cited by 44 · see citing works
Self-citationImpaired telomere maintenance in Alazami syndrome patients with LARP7 deficiency
Holohan, B., Kim, W., Lai, T., Hoshiyama, H., Zhang, N., Alazami, A. M., Wright, W. E., Meyn, M. S., Alkuraya, F. S., & Shay, J. W. (2016) · BMC Genomics · doi:10.1186/s12864-016-3093-4 · Cited by 44 · see citing works
LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA expression in fission yeast
Mennie, A. K., Moser, B. A., & Nakamura, T. (2018) · Nature Communications · doi:10.1038/s41467-018-02874-0 · Cited by 42 · see citing works
LARP7 family proteins have conserved function in telomerase assembly
Collopy, L. C., Ware, T. L., Goncalves, T., Kongsstovu, S. Í., Yang, Q., Amelina, H., Pinder, C., Alenazi, A., Moiseeva, V., Pearson, S. R., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02296-4 · Cited by 42 · see citing works
Structural basis of 7SK RNA 5′-γ-phosphate methylation and retention by MePCE
Yang, Y., Eichhorn, C. D., Wang, Y., Cascio, D., & Feigon, J. F. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0188-z · Cited by 38 · see citing works
Singh, M., Choi, C., & Feigon, J. F. (2013) · RNA Biology · doi:10.4161/rna.23608 · Cited by 34 · see citing works
Molecular interactions of fission yeast Skp1 and its role in the DNA damage checkpoint
Lehmann, A., Katayama, S., Harrison, C., Dhut, S., Kitamura, K., McDonald, N. Q., & Toda, T. (2004) · Genes to Cells · doi:10.1111/j.1356-9597.2004.00730.x · Cited by 34 · see citing works
Interaction of 7SK with the Smn complex modulates snRNP production
Ji, C., Bader, J. M., Ramanathan, P., Hennlein, L., Meissner, F., Jablonka, S., Mann, M., Fischer, U., Sendtner, M., & Briese, M. (2021) · Nature Communications · doi:10.1038/s41467-021-21529-1 · Cited by 33 · see citing works
Life and Death of Yeast Telomerase RNA
Vasianovich, Y., & Wellinger, R. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.01.013 · Cited by 31 · see citing works
Pof8 is a La-related protein and a constitutive component of telomerase in fission yeast
Páez-Moscoso, D. J., Pan, L., Sigauke, R. F., Schroeder, M. R., Tang, W., & Baumann, P. (2018) · Nature Communications · doi:10.1038/s41467-017-02284-8 · Cited by 30 · see citing works
Self-citationThe Bin3 RNA methyltransferase targets 7SK RNA to control transcription and translation
Cosgrove, M. S., Ding, Y., Rennie, W. A., Lane, M. J., & Hanes, S. D. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1123 · Cited by 28 · see citing works
Diverse mechanisms for spliceosome-mediated 3′ end processing of telomerase RNA
Kannan, R., Helston, R. M., Dannebaum, R. O., & Baumann, P. (2015) · Nature Communications · doi:10.1038/ncomms7104 · Cited by 26 · see citing works
Self-citationPrevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA
Qi, X., Rand, D. P., Podlevsky, J. D., Li, Y., Axel Mosig, A., Stadler, P. F., & Chen, J. J. ‐. (2015) · Nature Communications · doi:10.1038/ncomms7105 · Cited by 24 · see citing works
Kannan, R., Hartnett, S., Voelker, R. B., Berglund, J. A., Staley, J. P., & Baumann, P. (2013) · Genes & Development · doi:10.1101/gad.212738.112 · Cited by 23 · see citing works
Self-citationStabilize and connect: the role of LARP7 in nuclear non-coding RNA metabolism
Hasler, D., Meister, G., & Fischer, U. (2020) · RNA Biology · doi:10.1080/15476286.2020.1767952 · Cited by 21 · see citing works
Quality-Control Mechanism for Telomerase RNA Folding in the Cell
Hu, X., Kim, J., Yu, C., Jun, H.-I., Liu, J., Sankaran, B., Huang, L., & Qiao, F. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108568 · Cited by 18 · see citing works
Basu, R. S., Eichhorn, C. D., Cheng, R., Peterson, R. D., & Feigon, J. F. (2020) · RNA Biology · doi:10.1080/15476286.2020.1836891 · Cited by 13 · see citing works
Porat, J., Baidouri, M. E., Grigull, J., Deragon, J., & Bayfield, M. A. (2022) · Nature Communications · doi:10.1038/s41467-022-28985-3 · Cited by 10 · see citing works
baumannlab/Sp_Paez_et_al_2021: Sp_Paez_et_al_2021
Baumannlab (2021) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.5707801 · Cited by 1 · see citing works
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- Authors
- Páez-Moscoso, D. J., Ho, D. V., Pan, L., Hildebrand, K., Jensen, K. L., Levy, M. J., Florens, L., & Baumann, P.
- Affiliations
- Stowers Institute for Medical Research (US)
- Johannes Gutenberg University Mainz (DE)
- Corresponding author
- Baumann, Peter
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2021-12-16
- OpenAlex
- W4200274034
- Cited by
- 2
- References
- 66
- Citations by year
- 2024: 1 · 2022: 1
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- telomerase biogenesis, telomerase reverse transcriptase, telomerase RNA, cap-binding protein, telomere maintenance, Schizosaccharomyces pombe, telomerase holoenzyme
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