The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
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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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
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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