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The SSU Processome Component Utp25p is a Pseudohelicase
Open accessPreprint — published as 10.17912/micropub.biology.000606 · Paper page
Abstract
RNA helicases are involved in nearly all aspects of RNA metabolism and factor prominently in ribosome assembly. The SSU processome includes 10 helicases and many helicase-cofactors. Together, they mediate the structural rearrangements that occur during ribosomal SSU assembly. During the identification of the SSU processome component Utp25, it was noticed that the protein displays some sequence similarity to DEAD-box RNA helicases and is essential for growth. Interestingly, mutational ablation showed that Utp25’s DEAD-box motifs are dispensable. Here, we use AlphaFold to show that Utp25 retains considerable structural similarity to DEAD-box helicases and is the first fully validated pseudohelicase.
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Cites
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
UCSF ChimeraX: Structure visualization for researchers, educators, and developers
Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2021) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,514
Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1061 · Cited by 7,850
Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Christie, C. H., Dalenberg, K., Di Costanzo, L., Duarte, J. M., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1038 · Cited by 1,581
Structure and Mechanism of Helicases and Nucleic Acid Translocases
Singleton, M. R., Dillingham, M. S., & Wigley, D. B. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052305.115300 · Cited by 1,274
From unwinding to clamping — the DEAD box RNA helicase family
Linder, P., & Jankowsky, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3154 · Cited by 1,174
DEAD-box proteins: the driving forces behind RNA metabolism
Rocak, S., & Linder, P. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1335 · Cited by 772
Ribosome Biogenesis in the Yeast Saccharomyces cerevisiae
Woolford, J. L., & Baserga, S. J. (2013) · Genetics · doi:10.1534/genetics.113.153197 · Cited by 757
A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis
Dragon, F., Gallagher, J. E. G., Compagnone-Post, P. A., Mitchell, B. M., Porwancher, K. A., Wehner, K. A., Wormsley, S., Settlage, R. E., Shabanowitz, J., Osheim, Y., et al. (2002) · Nature · doi:10.1038/nature00769 · Cited by 688
Using Dali for Protein Structure Comparison
Holm, L. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0270-6_3 · Cited by 605
Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
Caruthers, J. M., Johnson, E. R., & McKay, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.24.13080 · Cited by 300
The multiple functions of RNA helicases as drivers and regulators of gene expression
Bourgeois, C. F., Mortreux, F., & Auboeuf, D. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.50 · Cited by 297
DExD/H-box proteins and their partners: helping RNA helicases unwind
Silverman, A. M., Edwalds-Gilbert, G., & Lin, R.-J. (2003) · Gene · doi:10.1016/s0378-1119(03)00626-7 · Cited by 220
DEAD-box helicases as integrators of RNA, nucleotide and protein binding
Putnam, A. A., & Jankowsky, E. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.02.002 · Cited by 218
The small subunit processome in ribosome biogenesis—progress and prospects
Phipps, K. R., Charette, J. M., & Baserga, S. J. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.57 · Cited by 188
Self-citationChen, J., Ruan, H., Ng, S. M. E., Gao, C., Soo, H. M., Wu, W., Zhang, Z., Wen, Z., Lane, D. P., & Peng, J. (2005) · Genes & Development · doi:10.1101/gad.1366405 · Cited by 172
Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase
Theissen, B., Karow, A. R., Köhler, J. R., Gubaev, A., & Klostermeier, D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705488105 · Cited by 163
Nucleolar maturation of the human small subunit processome
Singh, S. K., Broeck, A. V., Miller, L., Chaker-Margot, M., & Klinge, S. (2021) · Science · doi:10.1126/science.abj5338 · Cited by 147
Unravelling the Mechanisms of RNA Helicase Regulation
Sloan, K. E., & Bohnsack, M. T. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.02.001 · Cited by 145
The complete structure of the small-subunit processome
Barandun, J., Chaker-Margot, M., Hunziker, M., Molloy, K. R., Chait, B. T., & Klinge, S. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3472 · Cited by 135
Tracing the origin and evolution of pseudokinases across the tree of life
Kwon, A., Scott, S. T., Taujale, R., Yeung, W., Kochut, K. J., Eyers, P. A., & Kannan, N. (2019) · Science Signaling · doi:10.1126/scisignal.aav3810 · Cited by 124
A structural biology community assessment of AlphaFold 2 applications
Akdel, M., Pires, D. E. V., Porta Pardo, E., Jänes, J., Zalevsky, A. O., Mészáros, B., Bryant, P., Good, L. L., Laskowski, R. A., Pozzati, G., et al. (2021) · doi:10.1101/2021.09.26.461876 · Cited by 122
3.2-Å-resolution structure of the 90S preribosome before A1 pre-rRNA cleavage
Cheng, J., Kellner, N., Berninghausen, O., Hurt, E., & Beckmann, R. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3476 · Cited by 115
Emerging concepts in pseudoenzyme classification, evolution, and signaling
Ribeiro, A. J. M., Das, S., Dawson, N. L., Zaru, R., Orchard, S. E., Thornton, J. M., Orengo, C. A., Zeqiraj, E., Murphy, J. M., & Eyers, P. A. (2019) · Science Signaling · doi:10.1126/scisignal.aat9797 · Cited by 95
There’s more to death than life: Noncatalytic functions in kinase and pseudokinase signaling
Mace, P. D., & Murphy, J. M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100705 · Cited by 94
The Helicase-Like Domains of Type III Restriction Enzymes Trigger Long-Range Diffusion Along DNA
Schwarz, F. W., Tóth, J., van Aelst, K., Cui, G., Clausing, S., Szczelkun, M. D., & Seidel, R. (2013) · Science · doi:10.1126/science.1231122 · Cited by 77
Bernstein, K. A., Granneman, S., Lee, A. V., Manickam, S., & Baserga, S. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1195-1208.2006 · Cited by 74
Yeast and human RNA helicases involved in ribosome biogenesis: Current status and perspectives
Rodríguez‐Galán, O., García-Gómez, J. J., & de la Cruz, J. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.01.007 · Cited by 73
Granneman, S. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl419 · Cited by 67
Granneman, S., Bernstein, K. A., Bleichert, F., & Baserga, S. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1183-1194.2006 · Cited by 67
When a helicase is not a helicase: dsDNA tracking by the motor protein EcoR124I
Stanley, L. K., Seidel, R., van der Scheer, C., Dekker, N. H., Szczelkun, M. D., & Dekker, C. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601104 · Cited by 61
RNA folding and functions of RNA helicases in ribosome biogenesis
Mitterer, V., & Pertschy, B. (2022) · RNA Biology · doi:10.1080/15476286.2022.2079890 · Cited by 48
The DEAD-box RNA helicase-like Utp25 is an SSU processome component
Charette, J. M., & Baserga, S. J. (2010) · RNA · doi:10.1261/rna.2359810 · Cited by 46
Self-citationGoldfeder, M. B., & Oliveira, C. C. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07701.x · Cited by 29
Targeting DEAD ‐box RNA helicases: The emergence of molecular staples
Naineni, S. K., Robert, F., Nagar, B., & Pelletier, J. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1738 · Cited by 28
The SSU processome interactome in Saccharomyces cerevisiae reveals novel protein subcomplexes
Vincent, N., Charette, J. M., & Baserga, S. J. (2017) · RNA · doi:10.1261/rna.062927.117 · Cited by 22
Self-citationDeinococcus radiodurans PriA is a Pseudohelicase
Lopper, M. E., Boone, J., & Morrow, C. S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133419 · Cited by 7
Metadata
- Authors
- Helwer, R., & Charette, J. M.
- Affiliations
- CancerCare Manitoba (CA)
- Corresponding author
- Charette, J. Michael
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2022-07-09
- OpenAlex
- W4284993352
- Cited by
- 1
- References
- 37
- Citations by year
- 2024: 1
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Funders
- Natural Sciences and Engineering Research Council of Canada (RGPIN-2016, rgpin-2016-06599)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- DEAD-box RNA helicase, RNA helicase, ribosome assembly, protein structure prediction, essential proteins
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