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Article: The ribosomal maturation factor P from Mycobacterium smegmatis facilitates the ribosomal biogenesis by binding to the small ribosomal protein S12

TitleThe ribosomal maturation factor P from Mycobacterium smegmatis facilitates the ribosomal biogenesis by binding to the small ribosomal protein S12
Authors
KeywordsMSMEG 2624
Mycobacterium smegmatis
RimP
RpsL
bacterial translation
Issue Date2019
PublisherElsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology. The Journal's web site is located at https://www.journals.elsevier.com/journal-of-biological-chemistry
Citation
Journal of Biological Chemistry, 2019, v. 294 n. 1, p. 372-378 How to Cite?
AbstractThe ribosomal maturation factor P (RimP) is a highly conserved protein in bacteria and has been shown to be important in ribosomal assembly in Escherichia coli Because of its central importance in bacterial metabolism, RimP represents a good potential target for drug design to combat human pathogens such as Mycobacterium tuberculosis However, to date, the only RimP structure available is the NMR structure of the ortholog in another bacterial pathogen, Streptococcus pneumoniae Here, we report a 2.2 Å resolution crystal structure of MSMEG_2624, the RimP ortholog in the close M. tuberculosis relative Mycobacterium smegmatis, and using in vitro binding assays, we show that MSMEG_2624 interacts with the small ribosomal protein S12, also known as RpsL. Further analyses revealed that the conserved residues in the linker region between the N- and C-terminal domains of MSMEG_2624 are essential for binding to RpsL. However, neither of the two domains alone was sufficient to form strong interactions with RpsL. More importantly, the linker region was essential for in vivo ribosomal biogenesis. Our study provides critical mechanistic insights into the role of RimP in ribosome biogenesis. We anticipate that the MSMEG_2624 crystal structure has the potential to be used for drug design to manage M. tuberculosis infections.
Persistent Identifierhttp://hdl.handle.net/10722/300310
ISSN
2020 Impact Factor: 5.157
2015 SCImago Journal Rankings: 3.151
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChu, T-
dc.contributor.authorWeng, X-
dc.contributor.authorLau, COK-
dc.contributor.authorKong, HK-
dc.contributor.authorLau, J-
dc.contributor.authorLi, S-
dc.contributor.authorPham, HQ-
dc.contributor.authorWang, R-
dc.contributor.authorZhang, L-
dc.contributor.authorKao, RYT-
dc.contributor.authorLau, KF-
dc.contributor.authorNgo, JCK-
dc.contributor.authorLau, TCK-
dc.date.accessioned2021-06-04T08:41:08Z-
dc.date.available2021-06-04T08:41:08Z-
dc.date.issued2019-
dc.identifier.citationJournal of Biological Chemistry, 2019, v. 294 n. 1, p. 372-378-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/300310-
dc.description.abstractThe ribosomal maturation factor P (RimP) is a highly conserved protein in bacteria and has been shown to be important in ribosomal assembly in Escherichia coli Because of its central importance in bacterial metabolism, RimP represents a good potential target for drug design to combat human pathogens such as Mycobacterium tuberculosis However, to date, the only RimP structure available is the NMR structure of the ortholog in another bacterial pathogen, Streptococcus pneumoniae Here, we report a 2.2 Å resolution crystal structure of MSMEG_2624, the RimP ortholog in the close M. tuberculosis relative Mycobacterium smegmatis, and using in vitro binding assays, we show that MSMEG_2624 interacts with the small ribosomal protein S12, also known as RpsL. Further analyses revealed that the conserved residues in the linker region between the N- and C-terminal domains of MSMEG_2624 are essential for binding to RpsL. However, neither of the two domains alone was sufficient to form strong interactions with RpsL. More importantly, the linker region was essential for in vivo ribosomal biogenesis. Our study provides critical mechanistic insights into the role of RimP in ribosome biogenesis. We anticipate that the MSMEG_2624 crystal structure has the potential to be used for drug design to manage M. tuberculosis infections.-
dc.languageeng-
dc.publisherElsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology. The Journal's web site is located at https://www.journals.elsevier.com/journal-of-biological-chemistry-
dc.relation.ispartofJournal of Biological Chemistry-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectMSMEG 2624-
dc.subjectMycobacterium smegmatis-
dc.subjectRimP-
dc.subjectRpsL-
dc.subjectbacterial translation-
dc.titleThe ribosomal maturation factor P from Mycobacterium smegmatis facilitates the ribosomal biogenesis by binding to the small ribosomal protein S12-
dc.typeArticle-
dc.identifier.emailKao, RYT: rytkao@hkucc.hku.hk-
dc.identifier.authorityKao, RYT=rp00481-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1074/jbc.RA118.002298-
dc.identifier.pmid30409901-
dc.identifier.pmcidPMC6322892-
dc.identifier.hkuros322725-
dc.identifier.volume294-
dc.identifier.issue1-
dc.identifier.spage372-
dc.identifier.epage378-
dc.identifier.isiWOS:000455105500038-
dc.publisher.placeUnited States-

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