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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1993-2-8
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pubmed:abstractText |
The highly specific endoribonuclease activities of RNase E (which processes ribosomal 9S RNA into p5S RNA) and RNase K (which initiates decay of the ompA mRNA) are inferred to play a central role in RNA processing and mRNA decay in Escherichia coli. In vivo both activities are affected by a conditional mutation of the ams/rne gene that seems to be complemented at nonpermissive temperatures by a fragment of the groEL gene. Analysis of the relationship between the two nucleases and the heat shock protein revealed that GroEL interacts functionally with an RNase E-like activity but not with an RNase K activity, a groEL mutation affected 9S RNA processing but not ompA mRNA cleavage, RNase E activity could be precipitated with an antibody against GroEL, and a highly purified GroEL preparation contained RNase E activity but not RNase K activity. When purifying RNase E activity, we obtained a preparation containing two major proteins of 60 and 17 kDa. The size and the N-terminal sequence identified the 60-kDa protein as GroEL.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1370457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1525471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1644765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1676490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1679318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1683763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1704367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1708438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1713205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1713283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-1915294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2011493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2202593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2413440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2477358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2528694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2573517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2578448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-2897629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-3045757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-3046939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-3280138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-3546264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-365352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-379349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-379350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-387765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-6179925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-6187001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-6198319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-6351925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8093559-6387508
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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 |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
90
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pubmed:geneSymbol |
ams,
groEL,
ompA,
rne
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
277-81
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8093559-Amino Acid Sequence,
pubmed-meshheading:8093559-Bacterial Outer Membrane Proteins,
pubmed-meshheading:8093559-Bacterial Proteins,
pubmed-meshheading:8093559-Bacteriophage T7,
pubmed-meshheading:8093559-Chaperonin 60,
pubmed-meshheading:8093559-Endoribonucleases,
pubmed-meshheading:8093559-Escherichia coli,
pubmed-meshheading:8093559-Genes, Bacterial,
pubmed-meshheading:8093559-Genetic Complementation Test,
pubmed-meshheading:8093559-Heat-Shock Proteins,
pubmed-meshheading:8093559-Molecular Sequence Data,
pubmed-meshheading:8093559-Mutagenesis,
pubmed-meshheading:8093559-Promoter Regions, Genetic,
pubmed-meshheading:8093559-RNA, Messenger,
pubmed-meshheading:8093559-Restriction Mapping,
pubmed-meshheading:8093559-Transcription, Genetic
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pubmed:year |
1993
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pubmed:articleTitle |
Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli.
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pubmed:affiliation |
Department of Bacteriology, Karolinska Institute, Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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