File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: The Caulobacter crescentus CgtAC Protein Cosediments with the Free 50S Ribosomal Subunit

TitleThe Caulobacter crescentus CgtAC Protein Cosediments with the Free 50S Ribosomal Subunit
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2004
PublisherAmerican Society for Microbiology
Citation
Journal of Bacteriology, 2004, v. 186 n. 2, p. 481-489 How to Cite?
AbstractThe Obg family of GTPases is widely conserved and predicted to play an as-yet-unknown role in translation. Recent reports provide circumstantial evidence that both eukaryotic and prokaryotic Obg proteins are associated with the large ribosomal subunit. Here we provide direct evidence that the Caulobacter crescentus CgtAC protein is associated with the free large (50S) ribosomal subunit but not with 70S monosomes or with translating ribosomes. In contrast to the Bacillus subtilis and Escherichia coli proteins, CtAC does not fractionate in a large complex by gel filtration, indicating a moderately weak association with the 50S subunit. Moreover, binding of CgtAC to the 50S particle is sensitive to salt concentration and buffer composition but not guanine nucleotide occupancy of CgtAC. Assays of epitope-tagged wild-type and mutant variants of CgtAC indicate that the C terminus of CgtAC is critical for 50S association. Interestingly, the addition of a C-terminal epitope tag also affected the ability of various CgtAC alleles to function in vivo. Depletion of CgtAC led to perturbations in the polysome profile, raising the possibility that CgtAC is involved in ribosome assembly or stability.
Persistent Identifierhttp://hdl.handle.net/10722/90831
ISSN
2015 Impact Factor: 3.198
2015 SCImago Journal Rankings: 2.216
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLin, Ben_HK
dc.contributor.authorThayer, DAen_HK
dc.contributor.authorMaddock, JRen_HK
dc.date.accessioned2010-09-17T10:09:02Z-
dc.date.available2010-09-17T10:09:02Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal of Bacteriology, 2004, v. 186 n. 2, p. 481-489en_HK
dc.identifier.issn0021-9193en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90831-
dc.description.abstractThe Obg family of GTPases is widely conserved and predicted to play an as-yet-unknown role in translation. Recent reports provide circumstantial evidence that both eukaryotic and prokaryotic Obg proteins are associated with the large ribosomal subunit. Here we provide direct evidence that the Caulobacter crescentus CgtAC protein is associated with the free large (50S) ribosomal subunit but not with 70S monosomes or with translating ribosomes. In contrast to the Bacillus subtilis and Escherichia coli proteins, CtAC does not fractionate in a large complex by gel filtration, indicating a moderately weak association with the 50S subunit. Moreover, binding of CgtAC to the 50S particle is sensitive to salt concentration and buffer composition but not guanine nucleotide occupancy of CgtAC. Assays of epitope-tagged wild-type and mutant variants of CgtAC indicate that the C terminus of CgtAC is critical for 50S association. Interestingly, the addition of a C-terminal epitope tag also affected the ability of various CgtAC alleles to function in vivo. Depletion of CgtAC led to perturbations in the polysome profile, raising the possibility that CgtAC is involved in ribosome assembly or stability.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Microbiologyen_HK
dc.relation.ispartofJournal of Bacteriologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleThe Caulobacter crescentus CgtAC Protein Cosediments with the Free 50S Ribosomal Subuniten_HK
dc.typeArticleen_HK
dc.identifier.emailLin, B:blin@hku.hken_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1128/JB.186.2.481-489.2004en_HK
dc.identifier.pmid14702318-
dc.identifier.pmcidPMC305748-
dc.identifier.scopuseid_2-s2.0-0346024113en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0346024113&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume186en_HK
dc.identifier.issue2en_HK
dc.identifier.spage481en_HK
dc.identifier.epage489en_HK
dc.identifier.isiWOS:000188066800026-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats