globalchange  > 气候变化与战略
DOI: 10.1073/pnas.2009607117
论文题名:
Selective translation by alternative bacterial ribosomes
作者: Chen Y.-X.; Xu Z.-Y.; Ge X.; Sanyal S.; Lu Z.J.; Javid B.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期:32
起始页码: 19487
结束页码: 19496
语种: 英语
英文关键词: Alternative ribosomes ; Mycobacterium ; Ribosome profiling
Scopus关键词: Article ; bacterial strain ; codon ; complex formation ; controlled study ; iron homeostasis ; Mycobacterium smegmatis ; nonhuman ; operon ; phenotype ; priority journal ; protein synthesis ; ribosome ; RNA translation ; wild type ; genetics ; growth, development and aging ; metabolism ; Mycobacterium smegmatis ; ribosomal subunit ; ribosome ; translation initiation ; bacterial protein ; iron ; ribosomal protein S18 ; ribosome protein ; Bacterial Proteins ; Iron ; Mycobacterium smegmatis ; Peptide Chain Initiation, Translational ; Protein Biosynthesis ; Ribosomal Proteins ; Ribosome Subunits ; Ribosomes
英文摘要: Alternative ribosome subunit proteins are prevalent in the genomes of diverse bacterial species, but their functional significance is controversial. Attempts to study microbial ribosomal heterogeneity have mostly relied on comparing wild-type strains with mutants in which subunits have been deleted, but this approach does not allow direct comparison of alternate ribosome isoforms isolated from identical cellular contexts. Here, by simultaneously purifying canonical and alternative RpsR ribosomes from Mycobacterium smegmatis, we show that alternative ribosomes have distinct translational features compared with their canonical counterparts. Both alternative and canonical ribosomes actively take part in protein synthesis, although they translate a subset of genes with differential efficiency as measured by ribosome profiling. We also show that alternative ribosomes have a relative defect in initiation complex formation. Furthermore, a strain of M. smegmatis in which the alternative ribosome protein operon is deleted grows poorly in iron-depleted medium, uncovering a role for alternative ribosomes in iron homeostasis. Our work confirms the distinct and nonredundant contribution of alternative bacterial ribosomes for adaptation to hostile environments. © 2020 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163412
Appears in Collections:气候变化与战略

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作者单位: Chen, Y.-X., Centre for Global Health and Infectious Diseases, Collaborative Innovation Centre for the Diagnosis and Treatment of Infectious Diseases, Tsinghua University, School of Medicine, Beijing, 100084, China, Division of Experimental Medicine, University of California, San Francisco, CA 94110, United States; Xu, Z.-Y., Centre for Global Health and Infectious Diseases, Collaborative Innovation Centre for the Diagnosis and Treatment of Infectious Diseases, Tsinghua University, School of Medicine, Beijing, 100084, China, Ministry of Education Key Laboratory of Bioinformatics, Center for Synthetic and Systems Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China; Ge, X., Department of Cell and Molecular Biology, Uppsala University, Uppsala, 75124, Sweden; Sanyal, S., Department of Cell and Molecular Biology, Uppsala University, Uppsala, 75124, Sweden; Lu, Z.J., Ministry of Education Key Laboratory of Bioinformatics, Center for Synthetic and Systems Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China; Javid, B., Centre for Global Health and Infectious Diseases, Collaborative Innovation Centre for the Diagnosis and Treatment of Infectious Diseases, Tsinghua University, School of Medicine, Beijing, 100084, China, Division of Experimental Medicine, University of California, San Francisco, CA 94110, United States, Beijing Advanced Innovation Center in Structural Biology, Beijing, 100084, China

Recommended Citation:
Chen Y.-X.,Xu Z.-Y.,Ge X.,et al. Selective translation by alternative bacterial ribosomes[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(32)
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