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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-2-27
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pubmed:abstractText |
The protein translocation ATPase of Escherichia coli, SecA protein, auto-regulates its translation by binding to its translation initiation region in geneX-secA mRNA. To analyze this regulation further the secondary structure of this portion of geneX-secA RNA was investigated utilizing structure-specific nucleases and chemical probing approaches. The results of this analysis were consistent with the existence of two adjacent helices, helix I and the lower portion of helix II, whose function in secA activation and repression, respectively, has been demonstrated. Binding of SecA protein to geneX-secA RNA or various mutant derivatives of this RNA was studied by measurement of affinity constants, RNA footprint analysis, and quantitation of auto-repression in vivo. This analysis showed that the SecA-binding site in geneX-secA RNA was remarkably large spanning a region of 96 nucleotides including a 3' portion of helix II, the secA translation initiation region and distal sequences. From the size of the SecA-binding site and the plasticity of its response to mutational alteration, it is suggested that SecA protein contains two distinct RNA-binding sites. Finally, it was shown that SecA binding was not sufficient to promote auto-regulation and that sequences both upstream (helix I) and within the binding site can contribute to auto-regulation without affecting SecA-binding affinity.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/SecA protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
142-52
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9020978-Adenosine Triphosphatases,
pubmed-meshheading:9020978-Bacterial Proteins,
pubmed-meshheading:9020978-Base Sequence,
pubmed-meshheading:9020978-Binding Sites,
pubmed-meshheading:9020978-Escherichia coli,
pubmed-meshheading:9020978-Escherichia coli Proteins,
pubmed-meshheading:9020978-Gene Expression Regulation, Bacterial,
pubmed-meshheading:9020978-Genes, Bacterial,
pubmed-meshheading:9020978-Membrane Transport Proteins,
pubmed-meshheading:9020978-Molecular Sequence Data,
pubmed-meshheading:9020978-Nucleic Acid Conformation,
pubmed-meshheading:9020978-Protein Biosynthesis,
pubmed-meshheading:9020978-RNA, Bacterial,
pubmed-meshheading:9020978-RNA, Messenger,
pubmed-meshheading:9020978-Sequence Deletion
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pubmed:year |
1997
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pubmed:articleTitle |
Identification of elements on GeneX-secA RNA of Escherichia coli required for SecA binding and secA auto-regulation.
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pubmed:affiliation |
Department of Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT 06459, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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