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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...

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Detalles Bibliográficos
Autores principales: Helwer, Rafe, Charette, J. Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2022
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.
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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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