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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
48
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pubmed:dateCreated |
1993-1-8
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pubmed:abstractText |
Formation of the tertiary base pair G1401:C1501, which brings together two universally present and highly sequence-conserved single-stranded segments of small subunit ribosomal RNA, is essential for ribosome function. It was previously reported that mutation of G1401 inactivated all in vitro functions of the ribosome [Cunningham et al. (1992) Biochemistry 31, 7629-7637]. Here we show that mutation of C1501 to G was equally inactivating but that the double mutant C1401:G1501 with the base pair reversed had virtually full activity for tRNA binding to the P, A, and I sites and for peptide bond formation. Initiation-dependent formation of the first peptide bond remained 70-85% inhibited, despite full 70S initiation complex formation ability as evidenced by the ability to form fMET-puromycin. These results suggest that the defect in formation of the first peptide bond lies in filling the initial A site, Ai, rather than the subsequent elongation A sites, Ae. An increased mobility around the anticodon was detected by UV cross-linking of the anticodon of P-site-bound tRNA to C1399 as well as to the expected C1400. These findings provide the first experimental evidence for the existence of the G1401:C1501 base pair and show that this base pair, located at the decoding site, is essential for function. The structural implications of tertiary base pair formation are discussed.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 16S,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12012-22
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:1280994-Base Sequence,
pubmed-meshheading:1280994-Binding Sites,
pubmed-meshheading:1280994-Cross-Linking Reagents,
pubmed-meshheading:1280994-Escherichia coli,
pubmed-meshheading:1280994-Molecular Sequence Data,
pubmed-meshheading:1280994-Mutation,
pubmed-meshheading:1280994-N-Formylmethionine,
pubmed-meshheading:1280994-Nucleic Acid Conformation,
pubmed-meshheading:1280994-RNA, Bacterial,
pubmed-meshheading:1280994-RNA, Ribosomal, 16S,
pubmed-meshheading:1280994-RNA, Transfer,
pubmed-meshheading:1280994-Ribosomes,
pubmed-meshheading:1280994-Transcription, Genetic
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pubmed:year |
1992
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pubmed:articleTitle |
Interaction between the two conserved single-stranded regions at the decoding site of small subunit ribosomal RNA is essential for ribosome function.
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pubmed:affiliation |
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
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pubmed:publicationType |
Journal Article
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