دورية أكاديمية
أعرض في EDS

B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA cleavage.

التفاصيل البيبلوغرافية
العنوان: B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA cleavage.
المؤلفون: Park EN; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA., Mackens-Kiani T; Gene Center and Department of Biochemistry, University of Munich, Munich, Germany., Berhane R; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA., Esser H; Gene Center and Department of Biochemistry, University of Munich, Munich, Germany., Erdenebat C; Gene Center and Department of Biochemistry, University of Munich, Munich, Germany., Burroughs AM; Computational Biology Branch, Intramural Research Program, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA., Berninghausen O; Gene Center and Department of Biochemistry, University of Munich, Munich, Germany., Aravind L; Computational Biology Branch, Intramural Research Program, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA., Beckmann R; Gene Center and Department of Biochemistry, University of Munich, Munich, Germany., Green R; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.; Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA., Buskirk AR; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA. buskirk@jhmi.edu.
المصدر: The EMBO journal [EMBO J] 2024 Feb; Vol. 43 (4), pp. 484-506. Date of Electronic Publication: 2023 Dec 14.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 8208664 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1460-2075 (Electronic) Linking ISSN: 02614189 NLM ISO Abbreviation: EMBO J Subsets: MEDLINE
أسماء مطبوعة: Publication: 2024- : [London] : Nature Publishing Group
Original Publication: Eynsham, Oxford, England : Published for the European Molecular Biology Organization by IRL Press, [c1982-
مواضيع طبية MeSH: Protein Biosynthesis* , Bacillus subtilis*/genetics , Bacillus subtilis*/metabolism, RNA, Messenger/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Ribosomes/metabolism ; Peptides/metabolism
مستخلص: Stalled ribosomes are rescued by pathways that recycle the ribosome and target the nascent polypeptide for degradation. In E. coli, these pathways are triggered by ribosome collisions through the recruitment of SmrB, a nuclease that cleaves the mRNA. In B. subtilis, the related protein MutS2 was recently implicated in ribosome rescue. Here we show that MutS2 is recruited to collisions by its SMR and KOW domains, and we reveal the interaction of these domains with collided ribosomes by cryo-EM. Using a combination of in vivo and in vitro approaches, we show that MutS2 uses its ABC ATPase activity to split ribosomes, targeting the nascent peptide for degradation through the ribosome quality control pathway. However, unlike SmrB, which cleaves mRNA in E. coli, we see no evidence that MutS2 mediates mRNA cleavage or promotes ribosome rescue by tmRNA. These findings clarify the biochemical and cellular roles of MutS2 in ribosome rescue in B. subtilis and raise questions about how these pathways function differently in diverse bacteria.
(© 2023. The Author(s).)
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معلومات مُعتمدة: GM136960 HHS | NIH | National Institute of General Medical Sciences (NIGMS); TRR174 Deutsche Forschungsgemeinschaft (DFG)
فهرسة مساهمة: Keywords: ABC ATPase; B. subtilis; MutS2; Ribosome Collisions; Ribosome Quality Control (RQC)
المشرفين على المادة: 0 (RNA, Messenger)
0 (Peptides)
تواريخ الأحداث: Date Created: 20240104 Date Completed: 20240219 Latest Revision: 20240229
رمز التحديث: 20240229
مُعرف محوري في PubMed: PMC10897456
DOI: 10.1038/s44318-023-00010-3
PMID: 38177497
قاعدة البيانات: MEDLINE
الوصف
تدمد:1460-2075
DOI:10.1038/s44318-023-00010-3