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  • Wang, LiState Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China; Department of Philosophy and Religious Studies, Peking University, Beijing, China (author)

Loss of a single methylation in 23S rRNA delays 50S assembly at multiple late stages and impairs translation initiation and elongation

  • Article/chapterEnglish2020

Publisher, publication year, extent ...

  • 2020-06-22
  • Proceedings of the National Academy of Sciences,2020
  • printrdacarrier

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  • LIBRIS-ID:oai:DiVA.org:uu-419573
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-419573URI
  • https://doi.org/10.1073/pnas.1914323117DOI

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  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

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  • Author contributions: N.G. designed research; W.W., W.L., X.G., and C.S.M. performedresearch; K.Y. contributed new reagents/analytic tools; W.W., W.L., X.G., C.S.M., S.S., andN.G. analyzed data; and W.W., W.L., X.G., C.S.M., S.S., and N.G. wrote the paper.
  • Ribosome biogenesis is a complex process, and dozens of factors are required to facilitate and regulate the subunit assembly in bacteria. The 2′-O-methylation of U2552 in 23S rRNA by methyltransferase RrmJ is a crucial step in late-stage assembly of the 50S subunit. Its absence results in severe growth defect and marked accumulation of pre50S assembly intermediates. In the present work, we employed cryoelectron microscopy to characterize a set of late-stage pre50S particles isolated from an  Escherichia coli  Δ rrmJ strain. These assembly intermediates (solved at 3.2 to 3.8 Å resolution) define a collection of late-stage particles on a progressive assembly pathway. Apart from the absence of L16, L35, and L36, major structural differences between these intermediates and the mature 50S subunit are clustered near the peptidyl transferase center, such as H38, H68-71, and H89-93. In addition, the ribosomal A-loop of the mature 50S subunit from Δ rrmJ  strain displays large local flexibility on nucleotides next to unmethylated U2552. Fast kinetics-based biochemical assays demonstrate that the Δ rrmJ  50S subunit is only 50% active and two times slower than the WT 50S subunit in rapid subunit association. While the Δ rrmJ 70S ribosomes show no defect in peptide bond formation, peptide release, and ribosome recycling, they translocate with 20% slower rate than the WT ribosomes in each round of elongation. These defects amplify during synthesis of the full-length proteins and cause overall defect in protein synthesis. In conclusion, our data reveal the molecular roles of U2552 methylation in both ribosome biogenesis and protein translation.

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  • Wanqiu, LiState Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China; Department of Biology, Southern University of Science and Technology, Shenzhen, Guangdong, China; Institute of Life Sciences, Southeast University, Nanjing, China (author)
  • Ge, XueliangUppsala universitet,Molekylärbiologi(Swepub:uu)xuege734 (author)
  • Kaige, YanState Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China; Structural Studies, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom (author)
  • Mandava, Chandra Sekhar,1978-Uppsala universitet,Molekylärbiologi(Swepub:uu)chsma839 (author)
  • Sanyal, SuparnaUppsala universitet,Molekylärbiologi(Swepub:uu)sucsa102 (author)
  • Gao, NingState Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China (author)
  • Yan, Kaige(author)
  • State Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China; Department of Philosophy and Religious Studies, Peking University, Beijing, ChinaState Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China; Department of Biology, Southern University of Science and Technology, Shenzhen, Guangdong, China; Institute of Life Sciences, Southeast University, Nanjing, China (creator_code:org_t)

Related titles

  • In:Proceedings of the National Academy of Sciences of the United States of America: Proceedings of the National Academy of Sciences117:27, s. 15609-156190027-84241091-6490

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Wanqiu, Li
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