Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/159364
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dc.contributor.authorGoh, Kwok Jianen_US
dc.contributor.authorEro, Ryaen_US
dc.contributor.authorYan, Xin-Fuen_US
dc.contributor.authorPark, Jung Eunen_US
dc.contributor.authorKundukad, Binuen_US
dc.contributor.authorZheng, Junen_US
dc.contributor.authorSze, Siu Kwanen_US
dc.contributor.authorGao, Yong-Guien_US
dc.date.accessioned2022-06-15T05:54:29Z-
dc.date.available2022-06-15T05:54:29Z-
dc.date.issued2021-
dc.identifier.citationGoh, K. J., Ero, R., Yan, X., Park, J. E., Kundukad, B., Zheng, J., Sze, S. K. & Gao, Y. (2021). Translational GTPase BipA is involved in the maturation of a large subunit of bacterial ribosome at suboptimal temperature. Frontiers in Microbiology, 12, 686049-. https://dx.doi.org/10.3389/fmicb.2021.686049en_US
dc.identifier.issn1664-302Xen_US
dc.identifier.urihttps://hdl.handle.net/10356/159364-
dc.description.abstractBPI-inducible protein A (BipA), a highly conserved paralog of the well-known translational GTPases LepA and EF-G, has been implicated in bacterial motility, cold shock, stress response, biofilm formation, and virulence. BipA binds to the aminoacyl-(A) site of the bacterial ribosome and establishes contacts with the functionally important regions of both subunits, implying a specific role relevant to the ribosome, such as functioning in ribosome biogenesis and/or conditional protein translation. When cultured at suboptimal temperatures, the Escherichia coli bipA genomic deletion strain (ΔbipA) exhibits defects in growth, swimming motility, and ribosome assembly, which can be complemented by a plasmid-borne bipA supplementation or suppressed by the genomic rluC deletion. Based on the growth curve, soft agar swimming assay, and sucrose gradient sedimentation analysis, mutation of the catalytic residue His78 rendered plasmid-borne bipA unable to complement its deletion phenotypes. Interestingly, truncation of the C-terminal loop of BipA exacerbates the aforementioned phenotypes, demonstrating the involvement of BipA in ribosome assembly or its function. Furthermore, tandem mass tag-mass spectrometry analysis of the ΔbipA strain proteome revealed upregulations of a number of proteins (e.g., DeaD, RNase R, CspA, RpoS, and ObgE) implicated in ribosome biogenesis and RNA metabolism, and these proteins were restored to wild-type levels by plasmid-borne bipA supplementation or the genomic rluC deletion, implying BipA involvement in RNA metabolism and ribosome biogenesis. We have also determined that BipA interacts with ribosome 50S precursor (pre-50S), suggesting its role in 50S maturation and ribosome biogenesis. Taken together, BipA demonstrates the characteristics of a bona fide 50S assembly factor in ribosome biogenesis.en_US
dc.description.sponsorshipMinistry of Education (MOE)en_US
dc.language.isoenen_US
dc.relationRG108/20en_US
dc.relation.ispartofFrontiers in Microbiologyen_US
dc.rights© 2021 Goh, Ero, Yan, Park, Kundukad, Zheng, Sze and Gao. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en_US
dc.subjectScience::Biological sciencesen_US
dc.titleTranslational GTPase BipA is involved in the maturation of a large subunit of bacterial ribosome at suboptimal temperatureen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.researchSingapore Centre for Environmental Life Sciences and Engineering (SCELSE)en_US
dc.identifier.doi10.3389/fmicb.2021.686049-
dc.description.versionPublished versionen_US
dc.identifier.pmid34326822-
dc.identifier.scopus2-s2.0-85111381584-
dc.identifier.volume12en_US
dc.identifier.spage686049en_US
dc.subject.keywordsRibosome Biogenesisen_US
dc.subject.keywordsLarge Subunit Maturationen_US
dc.description.acknowledgementThis work was supported by a Tier I grant RG108/20 (to Y-GG) from the Ministry of Education (MOE) of Singapore.en_US
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