Source:http://linkedlifedata.com/resource/pubmed/id/11327780
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-4-30
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pubmed:abstractText |
Interactions within the decoding center of the 30 S ribosomal subunit have been investigated by constructing all 15 possible mutations at nucleotides C1402 and A1500 in helix 44 of 16 S rRNA. As expected, most of the mutations resulted in highly deleterious phenotypes, consistent with the high degree of conservation of this region and its functional importance. A total of seven mutants were viable under conditions where the mutant ribosomes comprised 100 % of the ribosomal pool. A suppressor mutation specific for the C1402U-A1500G mutant was isolated at position 1520 in helix 45 of 16 S rRNA. In addition, lack of dimethylation of A1518/A1519 caused by mutation of the ksgA methylase enhanced the deleterious effect of many of the 1402/1500 mutations. These data suggest that a higher-order interaction between helices 44 and 45 in 16 S rRNA is important for the proper functioning of the ribosome. This is consistent with the recent high-resolution crystal structures of the 30 S subunit, which show a tertiary interaction between the 1402/1500 region of helix 44 and the dimethyl A stem loop.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aminoglycosides,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 16S,
http://linkedlifedata.com/resource/pubmed/chemical/kasugamycin,
http://linkedlifedata.com/resource/pubmed/chemical/ksgA methyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
308
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
457-63
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11327780-Aminoglycosides,
pubmed-meshheading:11327780-Anti-Bacterial Agents,
pubmed-meshheading:11327780-Base Sequence,
pubmed-meshheading:11327780-Conserved Sequence,
pubmed-meshheading:11327780-Drug Resistance, Microbial,
pubmed-meshheading:11327780-Escherichia coli,
pubmed-meshheading:11327780-Methylation,
pubmed-meshheading:11327780-Methyltransferases,
pubmed-meshheading:11327780-Molecular Sequence Data,
pubmed-meshheading:11327780-Mutation,
pubmed-meshheading:11327780-Nucleic Acid Conformation,
pubmed-meshheading:11327780-Plasmids,
pubmed-meshheading:11327780-Protein Subunits,
pubmed-meshheading:11327780-RNA, Bacterial,
pubmed-meshheading:11327780-RNA, Ribosomal, 16S,
pubmed-meshheading:11327780-Ribosomes,
pubmed-meshheading:11327780-Suppression, Genetic
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pubmed:year |
2001
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pubmed:articleTitle |
Mutational analysis of the conserved bases C1402 and A1500 in the center of the decoding domain of Escherichia coli 16 S rRNA reveals an important tertiary interaction.
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pubmed:affiliation |
Department of Molecular and Cell Biology and Biochemistry J. W. Wilson Laboratory, Brown University, 69 Brown Street Providence, RI 02912, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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