Source:http://linkedlifedata.com/resource/pubmed/id/18955063
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
2008-12-5
|
| pubmed:abstractText |
Genetic changes lead gradually to altered protein function, making deduction of the molecular basis for activity from a sequence difficult. Comparative studies provide insights into the functional consequences of specific changes. Here we present structural and biochemical studies of NtrC4, a sigma-54 activator from Aquifex aeolicus, and compare it with NtrC1 (a paralog) and NtrC (a homolog from Salmonella enterica) to provide insight into how a substantial change in regulatory mechanism may have occurred. Activity assays show that assembly of NtrC4's active oligomer is repressed by the N-terminal receiver domain, and that BeF3- addition (mimicking phosphorylation) removes this repression. Observation of assembly without activation for NtrC4 indicates that it is much less strongly repressed than NtrC1. The crystal structure of the unactivated receiver-ATPase domain combination shows a partially disrupted interface. NMR structures of the regulatory domain show that its activation mechanism is very similar to that of NtrC1. The crystal structure of the NtrC4 DNA-binding domain shows that it is dimeric and more similar in structure to NtrC than NtrC1. Electron microscope images of the ATPase-DNA-binding domain combination show formation of oligomeric rings. Sequence alignments provide insights into the distribution of activation mechanisms in this family of proteins.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
1089-8638
|
| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
31
|
| pubmed:volume |
384
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1058-75
|
| pubmed:meshHeading |
pubmed-meshheading:18955063-Adenosine Triphosphate,
pubmed-meshheading:18955063-Amino Acid Sequence,
pubmed-meshheading:18955063-Bacteria,
pubmed-meshheading:18955063-Bacterial Proteins,
pubmed-meshheading:18955063-Computational Biology,
pubmed-meshheading:18955063-Crystallography, X-Ray,
pubmed-meshheading:18955063-DNA, Bacterial,
pubmed-meshheading:18955063-Dimerization,
pubmed-meshheading:18955063-Evolution, Molecular,
pubmed-meshheading:18955063-Gene Expression Regulation, Bacterial,
pubmed-meshheading:18955063-Hydrolysis,
pubmed-meshheading:18955063-Magnetic Resonance Spectroscopy,
pubmed-meshheading:18955063-Molecular Sequence Data,
pubmed-meshheading:18955063-Protein Binding,
pubmed-meshheading:18955063-Protein Structure, Quaternary,
pubmed-meshheading:18955063-Protein Structure, Secondary,
pubmed-meshheading:18955063-Protein Structure, Tertiary,
pubmed-meshheading:18955063-Sequence Alignment,
pubmed-meshheading:18955063-Sequence Homology, Amino Acid,
pubmed-meshheading:18955063-Solutions,
pubmed-meshheading:18955063-Trans-Activators,
pubmed-meshheading:18955063-Transcription, Genetic
|
| pubmed:year |
2008
|
| pubmed:articleTitle |
Structure and regulatory mechanism of Aquifex aeolicus NtrC4: variability and evolution in bacterial transcriptional regulation.
|
| pubmed:affiliation |
Graduate Group in Biophysics, Physical Biosciences Division, Lawrence Berkeley National Laboratory and the Department of Chemistry, University of California, Berkeley, CA 94720, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
|