Linked Life Data

12740396

Source:http://linkedlifedata.com/resource/pubmed/id/12740396

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2003-5-12
pubmed:databankReference
pubmed:abstractText
The transcriptional regulator RcsB interacts with other coactivators to control the expression of biosynthetic operons in enterobacteria. While in a heterodimer complex with the regulator RcsA the RcsAB box consensus is recognized, DNA binding sites for RcsB without RcsA have also been identified. The conformation of RcsB might therefore be modulated upon interaction with various coactivators, resulting in the recognition of different DNA targets. We report the solution structure of the C-terminal DNA-binding domain of the RcsB protein from Erwinia amylovora spanning amino acid residues 129-215 solved by heteronuclear magnetic resonance (NMR) spectroscopy. The C-terminal domain is composed of four alpha-helices where two central helices form a helix-turn-helix motif similar to the structures of the regulatory proteins GerE, NarL, and TraR. Amino acid residues involved in the RcsA independent DNA binding of RcsB were identified by titration studies with a RcsAB box consensus fragment. Data obtained from NMR spectroscopy together with surface plasmon resonance measurements demonstrate that the RcsAB box is specifically recognized by the RcsAB heterodimer as well as by RcsB alone. However, the binding constant of RcsB alone at target promoters from Escherichia coli, E. amylovora, and Pantoea stewartii was approximately 1 order of magnitude higher compared with that of the RcsAB heterodimer. We present evidence that the obvious role of RcsA is not to alter the DNA binding specificity of RcsB but to stabilize RcsB-DNA complexes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17752-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:12740396-Amino Acid Motifs, pubmed-meshheading:12740396-Amino Acid Sequence, pubmed-meshheading:12740396-Bacterial Proteins, pubmed-meshheading:12740396-DNA, pubmed-meshheading:12740396-DNA-Binding Proteins, pubmed-meshheading:12740396-Databases as Topic, pubmed-meshheading:12740396-Dimerization, pubmed-meshheading:12740396-Dose-Response Relationship, Drug, pubmed-meshheading:12740396-Erwinia, pubmed-meshheading:12740396-Escherichia coli, pubmed-meshheading:12740396-Escherichia coli Proteins, pubmed-meshheading:12740396-Genotype, pubmed-meshheading:12740396-Kinetics, pubmed-meshheading:12740396-Magnetic Resonance Spectroscopy, pubmed-meshheading:12740396-Models, Molecular, pubmed-meshheading:12740396-Molecular Sequence Data, pubmed-meshheading:12740396-Oligonucleotides, pubmed-meshheading:12740396-Plasmids, pubmed-meshheading:12740396-Promoter Regions, Genetic, pubmed-meshheading:12740396-Protein Binding, pubmed-meshheading:12740396-Protein Structure, Tertiary, pubmed-meshheading:12740396-Surface Plasmon Resonance, pubmed-meshheading:12740396-Time Factors, pubmed-meshheading:12740396-Transcription Factors
pubmed:year
2003
pubmed:articleTitle
Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box.
pubmed:affiliation
Kemijski Institute, National Institute of Chemistry, Hajdrihova 19, P. O. Box 660, SI-1001 Ljubljana, Slovenia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't