دورية أكاديمية
A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis.
| العنوان: | A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis. |
|---|---|
| المؤلفون: | Takada H; Faculty of Life Sciences, Kyoto Sangyo University and Institute for Protein Dynamics, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan.; Department of Biotechnology, Toyama Prefectural University,5180 Kurokawa, Imizu, Toyama 939-0398, Japan.; Department of Experimental Medical Science, Lund University, 221 00 Lund, Sweden., Paternoga H; Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany., Fujiwara K; Faculty of Life Sciences, Kyoto Sangyo University and Institute for Protein Dynamics, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan., Nakamoto JA; Department of Experimental Medical Science, Lund University, 221 00 Lund, Sweden., Park EN; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA., Dimitrova-Paternoga L; Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany., Beckert B; Dubochet Center for Imaging (DCI) at EPFL, EPFL SB IPHYS DCI, Lausanne, Switzerland., Saarma M; University of Tartu, Institute of Technology, 50411 Tartu, Estonia., Tenson T; University of Tartu, Institute of Technology, 50411 Tartu, Estonia., Buskirk AR; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA., Atkinson GC; Department of Experimental Medical Science, Lund University, 221 00 Lund, Sweden.; Virus Centre, Lund University, Lund, Sweden., Chiba S; Faculty of Life Sciences, Kyoto Sangyo University and Institute for Protein Dynamics, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan., Wilson DN; Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany., Hauryliuk V; Department of Experimental Medical Science, Lund University, 221 00 Lund, Sweden.; Virus Centre, Lund University, Lund, Sweden.; Science for Life Laboratory, Lund, Sweden. |
| المصدر: | Nucleic acids research [Nucleic Acids Res] 2024 Aug 12; Vol. 52 (14), pp. 8483-8499. |
| نوع المنشور: | Journal Article |
| 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: | Bacillus subtilis*/genetics , Bacillus subtilis*/metabolism , Bacterial Proteins*/metabolism , Bacterial Proteins*/genetics , Ribosomes*/metabolism , Protein Biosynthesis*, Protein Domains ; Cryoelectron Microscopy ; Protein Binding ; RNA-Binding Proteins/metabolism ; RNA-Binding Proteins/genetics ; Models, Molecular ; RNA, Transfer, Amino Acyl |
| مستخلص: | Ribosomes trapped on mRNAs during protein synthesis need to be rescued for the cell to survive. The most ubiquitous bacterial ribosome rescue pathway is trans-translation mediated by tmRNA and SmpB. Genetic inactivation of trans-translation can be lethal, unless ribosomes are rescued by ArfA or ArfB alternative rescue factors or the ribosome-associated quality control (RQC) system, which in Bacillus subtilis involves MutS2, RqcH, RqcP and Pth. Using transposon sequencing in a trans-translation-incompetent B. subtilis strain we identify a poorly characterized S4-domain-containing protein YlmH as a novel potential RQC factor. Cryo-EM structures reveal that YlmH binds peptidyl-tRNA-50S complexes in a position analogous to that of S4-domain-containing protein RqcP, and that, similarly to RqcP, YlmH can co-habit with RqcH. Consistently, we show that YlmH can assume the role of RqcP in RQC by facilitating the addition of poly-alanine tails to truncated nascent polypeptides. While in B. subtilis the function of YlmH is redundant with RqcP, our taxonomic analysis reveals that in multiple bacterial phyla RqcP is absent, while YlmH and RqcH are present, suggesting that in these species YlmH plays a central role in the RQC. (© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.) |
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| معلومات مُعتمدة: | G-2021-2-063 Institute for Fermentation, Osaka; 20H05926 JSPS Grants-in-Aid for Scientific Research; R01 GM136960 United States GM NIGMS NIH HHS; 20220562 Crafoord foundation; PRG335 Estonian Research Council; Umeå Centre for Microbial Research; 2020-0037 Knut and Alice Wallenberg Foundation; Universität Hamburg; 20 0872 Pj Cancerfonden; Centre for Structural Systems Biology, Hamburg; WI3285/11-1 Deutsche Forschungsgemeinschaft; 2019-01085 Swedish Research Council; INST 152/772-1 DFG; JP1159335 JST, ACT X, Japan; GM136960 United States GF NIH HHS |
| المشرفين على المادة: | 0 (Bacterial Proteins) 0 (RNA-Binding Proteins) 0 (tRNA, peptidyl-) 0 (RNA, Transfer, Amino Acyl) |
| تواريخ الأحداث: | Date Created: 20240529 Date Completed: 20240811 Latest Revision: 20240822 |
| رمز التحديث: | 20240822 |
| مُعرف محوري في PubMed: | PMC11317155 |
| DOI: | 10.1093/nar/gkae399 |
| PMID: | 38811035 |
| قاعدة البيانات: | MEDLINE |
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