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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2005-12-21
pubmed:abstractText
Ribosomal protein L7/12 is crucial for the function of elongation factor G (EF-G) on the ribosome. Here, we report the localization of a site in the C-terminal domain (CTD) of L7/12 that is critical for the interaction with EF-G. Single conserved surface amino acids were replaced in the CTD of L7/12. Whereas mutations in helices 5 and 6 had no effect, replacements of V66, I69, K70, and R73 in helix 4 increased the Michaelis constant (KM) of EF-G.GTP for the ribosome, suggesting an involvement of these residues in EF-G binding. The mutations did not appreciably affect rapid single-round GTP hydrolysis and had no effect on tRNA translocation on the ribosome. In contrast, the release of inorganic phosphate (Pi) from ribosome-bound EF-G.GDP.Pi was strongly inhibited and became rate-limiting for the turnover of EF-G. The control of Pi release by interactions between EF-G and L7/12 appears to be important for maintaining the conformational coupling between EF-G and the ribosome for translocation and for timing the dissociation of the factor from the ribosome.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-10449736, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-10625623, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-10637222, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-10880458, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-10891280, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-1092342, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-11231892, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-12369843, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-12379123, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-12820965, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-12859903, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-14759365, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-14960595, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-15037065, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-15147176, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-15461445, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-15985150, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-15989950, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-3139080, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-320039, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-3309338, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-3516698, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-361078, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-3883346, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-3911279, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-4329351, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-4333515, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-5339543, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-6113539, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-6396504, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-7035682, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-788779, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-7892205, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-7918447, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-798035, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-8031761, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-8070396, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-8070397, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-8080098, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-8834773, http://linkedlifedata.com/resource/pubmed/commentcorrection/16292341-8985244
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4316-23
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:16292341-Phosphates, pubmed-meshheading:16292341-Mutation, pubmed-meshheading:16292341-Kinetics, pubmed-meshheading:16292341-Escherichia coli, pubmed-meshheading:16292341-Crystallography, X-Ray, pubmed-meshheading:16292341-Models, Molecular, pubmed-meshheading:16292341-Time Factors, pubmed-meshheading:16292341-RNA, Messenger, pubmed-meshheading:16292341-Ribosomes, pubmed-meshheading:16292341-Protein Binding, pubmed-meshheading:16292341-RNA, Transfer, pubmed-meshheading:16292341-Models, Biological, pubmed-meshheading:16292341-Hydrolysis, pubmed-meshheading:16292341-Guanosine Triphosphate, pubmed-meshheading:16292341-Ribosomal Proteins, pubmed-meshheading:16292341-Protein Transport, pubmed-meshheading:16292341-Escherichia coli Proteins, pubmed-meshheading:16292341-Plasmids, pubmed-meshheading:16292341-Peptide Elongation Factor G
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