rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1981-6-23
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pubmed:abstractText |
The relationship between methylation of adenine near the 3' end of 16-S ribosomal RNA and the activity of 30-S ribosomal subunits has been studied using 30-S subunits from kasugamycin-sensitive and kasugamycin-resistant bacteria. Analysis of the proteins of 30-S subunits by gel electrophoresis showed that the content of protein S1 in 30-S subunits from a kasugamycin-resistant strain was smaller than that in 30-S subunits from the parent strain. Although polyphenylalanine-synthetic activity of 30-S subunits from a kasugamycin-resistant strain previously methylated by a methylase purified from Escherichia Q13 was nearly equal to that of untreated 30-S subunits, both phenylalanine-synthetic activity and the content of protein S1 in the 30-S particles reconstituted from 23-S core particles and split proteins from the kasugamycin-resistant strain increased by prior methylation of 23-S core particles by the methylase. These results suggest that methylation of adenine near the 3' end of 16-S rRNA induces an increase of polypeptide-synthetic activity by the acceleration of binding of protein S1 to S1-depleted 30-S subunits.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenine,
http://linkedlifedata.com/resource/pubmed/chemical/Aminoglycosides,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/kasugamycin,
http://linkedlifedata.com/resource/pubmed/chemical/polyphenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S1
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
113
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
587-93
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:6163627-Adenine,
pubmed-meshheading:6163627-Aminoglycosides,
pubmed-meshheading:6163627-Anti-Bacterial Agents,
pubmed-meshheading:6163627-Bacterial Proteins,
pubmed-meshheading:6163627-Drug Resistance, Microbial,
pubmed-meshheading:6163627-Escherichia coli,
pubmed-meshheading:6163627-Methylation,
pubmed-meshheading:6163627-Peptide Biosynthesis,
pubmed-meshheading:6163627-Peptides,
pubmed-meshheading:6163627-RNA, Bacterial,
pubmed-meshheading:6163627-RNA, Ribosomal,
pubmed-meshheading:6163627-Ribosomal Proteins,
pubmed-meshheading:6163627-Ribosomes
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pubmed:year |
1981
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pubmed:articleTitle |
Relationship between methylation of adenine near the 3' end of 16-S ribosomal RNA and the activity of 30-S ribosomal subunits.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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