Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-8-24
pubmed:abstractText
Obg is a GTP-binding protein of Bacillus subtilis with essential, but undefined roles in the bacterium's growth, sporulation, and stress responses. Obg orthologs are widely conserved among both bacteria and eukaryotes. Gel filtration and affinity blot assays have suggested that Obg may be ribosome-associated. In the current work, we continue an examination of the putative Obg:ribosome interaction. Velocity centrifugation analyses of crude B. subtilis extracts or purified Obg:ribosome mixtures suggest that Obg is initially ribosome-bound, but can separate from ribosomes during sedimentation in the absence of added nucleotides. Addition of either GTP, GDP or ATP to the gradient prolonged the Obg:ribosome association, while inclusion of a nonhydrolyzable GTP analog (5-guanylyl-imidodiphosphate) preserved it. The data strengthen the notion that Obg is a ribosome-associated protein, demonstrate that Obg's association with ribosomes is stabilized by GTP, and indicate that the ribosome-bound Obg can likely hydrolyze GTP and be released as a consequence.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
322
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
565-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to ribosomes.
pubmed:affiliation
Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, TX 78229-3900, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't