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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 |
2004-1-20
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pubmed:databankReference |
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pubmed:abstractText |
The cI protein of bacteriophage lambda (lambdacI) activates transcription by binding a DNA operator just upstream of the promoter and interacting with the RNA polymerase sigma subunit domain 4 (sigma(4)). We determined the crystal structure of the lambdacI/sigma(4)/DNA ternary complex at 2.3 A resolution. There are no conformational changes in either protein, which interact through an extremely small interface involving at most 6 amino acid residues. The interactions of the two proteins stabilize the binding of each protein to the DNA. The results provide insight into how activators can operate through a simple cooperative binding mechanism but affect different steps of the transcription initiation process.
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pubmed:grant |
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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 |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45-53
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:14731393-Amino Acid Sequence,
pubmed-meshheading:14731393-Bacteriophage lambda,
pubmed-meshheading:14731393-Base Sequence,
pubmed-meshheading:14731393-Consensus Sequence,
pubmed-meshheading:14731393-Crystallography, X-Ray,
pubmed-meshheading:14731393-DNA-Binding Proteins,
pubmed-meshheading:14731393-DNA-Directed RNA Polymerases,
pubmed-meshheading:14731393-Escherichia coli,
pubmed-meshheading:14731393-Holoenzymes,
pubmed-meshheading:14731393-Hydrogen Bonding,
pubmed-meshheading:14731393-Models, Molecular,
pubmed-meshheading:14731393-Molecular Sequence Data,
pubmed-meshheading:14731393-Promoter Regions, Genetic,
pubmed-meshheading:14731393-Protein Binding,
pubmed-meshheading:14731393-Sigma Factor,
pubmed-meshheading:14731393-Transcription, Genetic,
pubmed-meshheading:14731393-Transcriptional Activation
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pubmed:year |
2004
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pubmed:articleTitle |
Structure of a ternary transcription activation complex.
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pubmed:affiliation |
The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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