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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1988-11-8
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pubmed:abstractText |
gamma-Amides of GTP and affinity and photoaffinity derivatives of gamma-amides of GTP: gamma-anilide of GTP, gamma-(4-azido)anilide of GTP, gamma-[N-(4-azidobenzyl)-N-methyl]amide of GTP, gamma[4-N-(2-chloroethyl)-N-methylaminobenzyl]amide of GTP and gamma-[4-N-(2-oxoethyl)-N-methylaminobenzyl]amide of GTP substituted efficiently for GTP in the EF-Tu-dependent transfer of aminoacyl-tRNA to the ribosome but, in contrast to GTP, they were not hydrolyzed in this process. They represent a new class of non-hydrolyzable GTP analogs with preserved gamma-phosphodiester bond. The radioactive analog of GTP: gamma-[4-N-(2-chloroethyl)-N-methylamino[14C]benzyl]amide of GTP was used as an affinity labeling probe for the identification of components of the GTPase center formed in the EF-Tu-dependent transfer reaction of aminoacyl-tRNA to the ribosomal A-site. Within a six-component complex of poly(U)-programmed E. coli ribosomes with elongation factor Tu, Phe-tRNA(Phe) (at the A-site), tRNA(Phe) (at the P-site) and the [14C]GTP analog, mainly the ribosomal 23S RNA and to a lesser extent the ribosomal proteins L17, L21, S16, S21 and the ribosomal 16S RNA were labeled by the reagent. No significant modification of EF-Tu was detected.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/(4-N-(2-chloroethyl)-N-methylaminobe...,
http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Amides,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolase-Linked...,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor Tu,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/polyphenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, phenylalanine-
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0300-9084
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
597-603
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:3139078-Affinity Labels,
pubmed-meshheading:3139078-Amides,
pubmed-meshheading:3139078-Binding Sites,
pubmed-meshheading:3139078-Escherichia coli,
pubmed-meshheading:3139078-GTP Phosphohydrolase-Linked Elongation Factors,
pubmed-meshheading:3139078-Guanosine Triphosphate,
pubmed-meshheading:3139078-Hydrolysis,
pubmed-meshheading:3139078-Peptide Biosynthesis,
pubmed-meshheading:3139078-Peptide Elongation Factor Tu,
pubmed-meshheading:3139078-Peptides,
pubmed-meshheading:3139078-Photochemistry,
pubmed-meshheading:3139078-RNA, Transfer, Amino Acyl,
pubmed-meshheading:3139078-Ribosomes
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pubmed:year |
1988
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pubmed:articleTitle |
Affinity labeling at the A-site of Escherichia coli ribosomes by a non-hydrolyzable gamma-amide analog of GTP.
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pubmed:affiliation |
Institute of Bioorganic Chemistry, Siberian Division of the Academy of Sciences, Novosibirsk, U.S.S.R.
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pubmed:publicationType |
Journal Article
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