Linked Life Data

15876365

Source:http://linkedlifedata.com/resource/pubmed/id/15876365

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-5-6
pubmed:databankReference
pubmed:abstractText
Escherichia coli react to changes from aerobic to anaerobic conditions of growth using the ArcA-ArcB two-component signal transduction system. This system, in conjunction with other proteins, regulates the respiratory metabolic pathways in the organism. ArcA is a member of the OmpR/PhoB subfamily of response regulator transcription factors that are known to regulate transcription by binding in tandem to target DNA direct repeats. It is still unclear in this subfamily how activation by phosphorylation of the regulatory domain of response regulators stimulates DNA binding by the effector domain and how dimerization and domain orientation, as well as intra- and intermolecular interactions, affect this process. In order to address these questions we have solved the crystal structures of the regulatory domain of ArcA in the presence and absence of the phosphoryl analog, BeF3-. In the crystal structures, the regulatory domain of ArcA forms a symmetric dimer mediated by the alpha4-beta5-alpha5 face of the protein and involving a number of residues that are highly conserved in the OmpR/PhoB subfamily. It is hypothesized that members of this subfamily use a common mechanism of regulation by dimerization. Additional biophysical studies were employed to probe the oligomerization state of ArcA, as well as its individual domains, in solution. The solution studies show the propensity of the individual domains to associate into oligomers larger than the dimer observed for the intact protein, and suggest that the C-terminal DNA-binding domain also plays a role in oligomerization.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
349
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-26
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:15876365-Amino Acid Sequence, pubmed-meshheading:15876365-Bacterial Outer Membrane Proteins, pubmed-meshheading:15876365-Beryllium, pubmed-meshheading:15876365-Binding Sites, pubmed-meshheading:15876365-Chromatography, Liquid, pubmed-meshheading:15876365-Dimerization, pubmed-meshheading:15876365-Escherichia coli, pubmed-meshheading:15876365-Escherichia coli Proteins, pubmed-meshheading:15876365-Fluorides, pubmed-meshheading:15876365-Hydrophobic and Hydrophilic Interactions, pubmed-meshheading:15876365-Molecular Sequence Data, pubmed-meshheading:15876365-Phosphorylation, pubmed-meshheading:15876365-Protein Structure, Secondary, pubmed-meshheading:15876365-Protein Structure, Tertiary, pubmed-meshheading:15876365-Repressor Proteins, pubmed-meshheading:15876365-Sequence Alignment, pubmed-meshheading:15876365-Ultracentrifugation
pubmed:year
2005
pubmed:articleTitle
Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.
pubmed:affiliation
Department of Chemistry and Chemical Biology, Rutgers University, 610 Taylor Road, Piscataway, NJ 08854, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural