دورية أكاديمية
أعرض في EDS

Yeast Ssd1 is a non-enzymatic member of the RNase II family with an alternative RNA recognition site.

التفاصيل البيبلوغرافية
العنوان: Yeast Ssd1 is a non-enzymatic member of the RNase II family with an alternative RNA recognition site.
المؤلفون: Bayne RA; Institute of Cell Biology and SynthSys, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK., Jayachandran U; Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK., Kasprowicz A; Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK., Bresson S; Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK., Tollervey D; Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK., Wallace EWJ; Institute of Cell Biology and SynthSys, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK., Cook AG; Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
المصدر: Nucleic acids research [Nucleic Acids Res] 2022 Mar 21; Vol. 50 (5), pp. 2923-2937.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE
أسماء مطبوعة: Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.
مواضيع طبية MeSH: Exoribonucleases*/metabolism , Saccharomyces cerevisiae*/metabolism , Saccharomyces cerevisiae Proteins*/genetics , Saccharomyces cerevisiae Proteins*/metabolism, 5' Untranslated Regions ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
مستخلص: Ssd1, a conserved fungal RNA-binding protein, is important in stress responses, cell division and virulence. Ssd1 is closely related to Dis3L2 of the RNase II family of nucleases, but lacks catalytic activity and likely suppresses translation of bound mRNAs. Previous studies identified RNA motifs enriched in Ssd1-associated transcripts, yet the sequence requirements for Ssd1 binding are not defined. Here, we identify precise binding sites of Ssd1 on RNA using in vivo cross-linking and cDNA analysis. These sites are enriched in 5' untranslated regions of a subset of mRNAs encoding cell wall proteins. We identified a conserved bipartite motif that binds Ssd1 with high affinity in vitro. Active RNase II enzymes have a characteristic, internal RNA binding path; the Ssd1 crystal structure at 1.9 Å resolution shows that remnants of regulatory sequences block this path. Instead, RNA binding activity has relocated to a conserved patch on the surface of the protein. Structure-guided mutations of this surface prevent Ssd1 from binding RNA in vitro and phenocopy Ssd1 deletion in vivo. These studies provide a new framework for understanding the function of a pleiotropic post-transcriptional regulator of gene expression and give insights into the evolution of regulatory and binding elements in the RNase II family.
(© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.)
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معلومات مُعتمدة: 203149 United Kingdom WT_ Wellcome Trust; 200898/Z/16/Z United Kingdom WT_ Wellcome Trust; 109916/Z/15/Z United Kingdom WT_ Wellcome Trust; 109916 United Kingdom WT_ Wellcome Trust; 208779 United Kingdom WT_ Wellcome Trust; 200898 United Kingdom WT_ Wellcome Trust; 208779/Z/17/Z United Kingdom WT_ Wellcome Trust
المشرفين على المادة: 0 (5' Untranslated Regions)
0 (RNA, Messenger)
0 (Saccharomyces cerevisiae Proteins)
0 (Ssd1 protein, S cerevisiae)
EC 3.1.- (Exoribonucleases)
EC 3.1.13.1 (exoribonuclease II)
تواريخ الأحداث: Date Created: 20210724 Date Completed: 20220415 Latest Revision: 20230222
رمز التحديث: 20230222
مُعرف محوري في PubMed: PMC8934651
DOI: 10.1093/nar/gkab615
PMID: 34302485
قاعدة البيانات: MEDLINE
الوصف
تدمد:1362-4962
DOI:10.1093/nar/gkab615