Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2007-8-6
pubmed:databankReference
pubmed:abstractText
Rho-dependent transcription termination is an essential process for the regulation of bacterial gene expression. Thus far, only two Rho-specific inhibitors of bacterial transcription termination have been described, the psu protein from the satellite bacteriophage P4 and YaeO from Escherichia coli. Here, we report the solution structure of YaeO, the first of a Rho-specific inhibitor of transcription termination. YaeO is an acidic protein composed of an N-terminal helix and a seven-stranded beta sandwich. NMR chemical shift perturbation experiments revealed that YaeO binds proximal to the primary nucleic acid binding site of Rho. Based on the NMR titrations, a docked model of the YaeO-Rho complex was calculated. These results suggest that YaeO binds outside the Rho hexamer, acting as a competitive inhibitor of RNA binding. In vitro gel shift assays confirmed the inhibition of nucleic acid binding to Rho. Site-directed mutagenesis showed that the negative character of YaeO is essential for its function in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23348-53
pubmed:meshHeading
pubmed-meshheading:17565995-Amino Acid Sequence, pubmed-meshheading:17565995-Binding, Competitive, pubmed-meshheading:17565995-Escherichia coli, pubmed-meshheading:17565995-Escherichia coli Proteins, pubmed-meshheading:17565995-Magnetic Resonance Spectroscopy, pubmed-meshheading:17565995-Models, Biological, pubmed-meshheading:17565995-Models, Molecular, pubmed-meshheading:17565995-Molecular Conformation, pubmed-meshheading:17565995-Molecular Sequence Data, pubmed-meshheading:17565995-Mutagenesis, Site-Directed, pubmed-meshheading:17565995-Protein Conformation, pubmed-meshheading:17565995-Protein Structure, Secondary, pubmed-meshheading:17565995-Protein Structure, Tertiary, pubmed-meshheading:17565995-Sequence Homology, Amino Acid, pubmed-meshheading:17565995-beta-Galactosidase, pubmed-meshheading:17565995-rho GTP-Binding Proteins
pubmed:year
2007
pubmed:articleTitle
Solution structure of YaeO, a Rho-specific inhibitor of transcription termination.
pubmed:affiliation
Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't