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Article: The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with spot, a ppGpp synthetase/hydrolase

TitleThe Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with spot, a ppGpp synthetase/hydrolase
Authors
KeywordsSpecies Index: Bacteria (Microorganisms)
Caulobacter Vibrioides
Escherichia Coli
Negibacteria
Issue Date2004
PublisherAmerican Society for Microbiology
Citation
Journal of Bacteriology, 2004, v. 186 n. 16, p. 5249-5257 How to Cite?
AbstractCgtAE/ObgE/YhbZ is an Escherichia coli guanine nucleotide binding protein of the Obg/GTP1 subfamily whose members have been implicated in a number of cellular functions including GTP-GDP sensing, sporulation initiation, and translation. Here we describe a kinetic analysis of CgtAE with guanine nucleotides and show that its properties are similar to those of the Caulobacter crescentus homolog CgtAC. CgtAE binds both GTP and GDP with moderate affinity, shows high guanine nucleotide exchange rate constants for both nucleotides, and has a relatively low GTP hydrolysis rate. We show that CgtAE is associated predominantly with the 50S ribosomal subunit. Interestingly, CgtAE copurifies with SpoT, a ribosome-associated ppGpp hydrolase/synthetase involved in the stress response. The interaction between CgtAE and SpoT was confirmed by reciprocal coprecipitation experiments and by two-hybrid assays. These studies raise the possibility that the ribosome-associated CgtA E is involved in the SpoT-mediated stress response.
Persistent Identifierhttp://hdl.handle.net/10722/90865
ISSN
2015 Impact Factor: 3.198
2015 SCImago Journal Rankings: 2.216
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWout, Pen_HK
dc.contributor.authorPu, Ken_HK
dc.contributor.authorSullivan, SMen_HK
dc.contributor.authorReese, Ven_HK
dc.contributor.authorZhou, Sen_HK
dc.contributor.authorLin, Ben_HK
dc.contributor.authorMaddock, JRen_HK
dc.date.accessioned2010-09-17T10:09:32Z-
dc.date.available2010-09-17T10:09:32Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal of Bacteriology, 2004, v. 186 n. 16, p. 5249-5257en_HK
dc.identifier.issn0021-9193en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90865-
dc.description.abstractCgtAE/ObgE/YhbZ is an Escherichia coli guanine nucleotide binding protein of the Obg/GTP1 subfamily whose members have been implicated in a number of cellular functions including GTP-GDP sensing, sporulation initiation, and translation. Here we describe a kinetic analysis of CgtAE with guanine nucleotides and show that its properties are similar to those of the Caulobacter crescentus homolog CgtAC. CgtAE binds both GTP and GDP with moderate affinity, shows high guanine nucleotide exchange rate constants for both nucleotides, and has a relatively low GTP hydrolysis rate. We show that CgtAE is associated predominantly with the 50S ribosomal subunit. Interestingly, CgtAE copurifies with SpoT, a ribosome-associated ppGpp hydrolase/synthetase involved in the stress response. The interaction between CgtAE and SpoT was confirmed by reciprocal coprecipitation experiments and by two-hybrid assays. These studies raise the possibility that the ribosome-associated CgtA E is involved in the SpoT-mediated stress response.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Microbiologyen_HK
dc.relation.ispartofJournal of Bacteriologyen_HK
dc.subjectSpecies Index: Bacteria (Microorganisms)en_HK
dc.subjectCaulobacter Vibrioidesen_HK
dc.subjectEscherichia Colien_HK
dc.subjectNegibacteriaen_HK
dc.titleThe Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with spot, a ppGpp synthetase/hydrolaseen_HK
dc.typeArticleen_HK
dc.identifier.emailLin, B:blin@hku.hken_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1128/JB.186.16.5249-5257.2004en_HK
dc.identifier.pmid15292126-
dc.identifier.pmcidPMC490892-
dc.identifier.scopuseid_2-s2.0-3843074167en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-3843074167&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume186en_HK
dc.identifier.issue16en_HK
dc.identifier.spage5249en_HK
dc.identifier.epage5257en_HK
dc.identifier.isiWOS:000223179000009-
dc.identifier.f10001020617-

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