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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
1990-11-13
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pubmed:abstractText |
The 30S ribosomal subunits derived from Escherichia coli TA114, a a temperature-sensitive mutant lacking ribosomal protein S20, were shown to be defective in two ways: (a) they have a reduced capacity for association with the 50S ribosomal subunit which results in the impairment of most of the functions requiring a coordinated interaction between the two subunits; (b) they are defective in functions which do not require their interaction with the large subunit (i.e., the formation of ternary complexes with aminocyl-tRNAs and templates, including the formation of 30S initiation complexes with fMet-tRNA and mRNA). The 30S (-S20) subunits seem to interact normally with both template and aminoacyl-tRNA individually, but appear to be impaired in the rate-limiting isomerization step leading to the formation of a codon-anticodon interaction in the P site.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
1050
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
93-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2207174-Kinetics,
pubmed-meshheading:2207174-Mutation,
pubmed-meshheading:2207174-Peptide Biosynthesis,
pubmed-meshheading:2207174-Peptide Chain Initiation, Translational,
pubmed-meshheading:2207174-Peptides,
pubmed-meshheading:2207174-Poly U,
pubmed-meshheading:2207174-RNA, Transfer, Amino Acyl,
pubmed-meshheading:2207174-Ribosomal Proteins,
pubmed-meshheading:2207174-Ribosomes,
pubmed-meshheading:2207174-Temperature
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pubmed:year |
1990
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pubmed:articleTitle |
Escherichia coli 30S mutants lacking protein S20 are defective in translation initiation.
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pubmed:affiliation |
Max-Planck-Institut für Molekulare Genetik, Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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