Translational GTPase BipA Is Involved in the Maturation of a Large Subunit of Bacterial Ribosome at Suboptimal Temperature.

Autor:	Goh KJ; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore., Ero R; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore., Yan XF; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore., Park JE; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore., Kundukad B; Singapore Centre for Environmental Life Sciences Engineering, Nanyang Technological University, Singapore, Singapore., Zheng J; Faculty of Health Sciences, University of Macau, Macau, China., Sze SK; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore., Gao YG; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Jazyk:	angličtina
Zdroj:	Frontiers in microbiology [Front Microbiol] 2021 Jul 13; Vol. 12, pp. 686049. Date of Electronic Publication: 2021 Jul 13 (Print Publication: 2021).
DOI:	10.3389/fmicb.2021.686049
Abstrakt:	BPI-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 (Δ bipA ) 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 Δ bipA 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. Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. (Copyright © 2021 Goh, Ero, Yan, Park, Kundukad, Zheng, Sze and Gao.)
Databáze:	MEDLINE
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