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The SSU Processome Component Utp25p is a Pseudohelicase
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 as part of ribosomal SSU assembly. During the identifi...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Caltech Library
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9539457/ https://www.ncbi.nlm.nih.gov/pubmed/36212518 http://dx.doi.org/10.17912/micropub.biology.000606 |
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author | Helwer, Rafe Charette, J. Michael |
author_facet | Helwer, Rafe Charette, J. Michael |
author_sort | Helwer, Rafe |
collection | PubMed |
description | 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 as part of ribosomal SSU assembly. During the identification of the SSU processome component Utp25/Def, 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 show that the Utp25 AlphaFold prediction displays considerable structural similarity to DEAD-box helicases and is the first fully validated pseudohelicase. |
format | Online Article Text |
id | pubmed-9539457 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Caltech Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-95394572022-10-08 The SSU Processome Component Utp25p is a Pseudohelicase Helwer, Rafe Charette, J. Michael MicroPubl Biol New Finding 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 as part of ribosomal SSU assembly. During the identification of the SSU processome component Utp25/Def, 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 show that the Utp25 AlphaFold prediction displays considerable structural similarity to DEAD-box helicases and is the first fully validated pseudohelicase. Caltech Library 2022-09-22 /pmc/articles/PMC9539457/ /pubmed/36212518 http://dx.doi.org/10.17912/micropub.biology.000606 Text en Copyright: © 2022 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | New Finding Helwer, Rafe Charette, J. Michael The SSU Processome Component Utp25p is a Pseudohelicase |
title | The SSU Processome Component Utp25p is a Pseudohelicase |
title_full | The SSU Processome Component Utp25p is a Pseudohelicase |
title_fullStr | The SSU Processome Component Utp25p is a Pseudohelicase |
title_full_unstemmed | The SSU Processome Component Utp25p is a Pseudohelicase |
title_short | The SSU Processome Component Utp25p is a Pseudohelicase |
title_sort | ssu processome component utp25p is a pseudohelicase |
topic | New Finding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9539457/ https://www.ncbi.nlm.nih.gov/pubmed/36212518 http://dx.doi.org/10.17912/micropub.biology.000606 |
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