Linked Life Data

17609131

Source:http://linkedlifedata.com/resource/pubmed/id/17609131

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2007-7-4
pubmed:abstractText
Escherichia coli histidine kinases play an essential role in sensing external environmental changes. Since the majority of these are transmembrane proteins, it is believed that their periplasmic domains function as receptor and transduce a signal through the transmembrane domain to their cytoplasmic enzymatic domains. Therefore, it is important to understand how signal transduction modulates the enzymatic activities of histidine kinase across transmembrane. Osmosensor histidine kinase EnvZ and chemoreceptor Tar are well-characterized signal-transducing proteins; a fusion of these two proteins would prove to be an ideal tool not only for characterization of histidine kinase EnvZ, but also, more importantly, as a general approach for studying the molecular mechanism of signal transduction across transmembranes. Tar-EnvZ chimeric protein served as a useful tool to study how the signal modulates enzymatic activities of EnvZ by using a well-defined chemical, aspartate, as a receptor ligand. As more and more genome sequences are being published, the number of identified histidine kinases is rapidly growing. The analysis of these newly identified histidine kinases revealed that the architecture of their cytoplasmic domains is more complex than was perceived based on E. coli histidine kinases. Therefore, chimeric proteins of these histidine kinases with Tar receptor would be helpful to study the mechanism of signal transduction. This chapter describes methods for designing chimeric proteins between a histidine kinase of interest and the Tar receptor and applications of the chimeric protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
423
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
166-83
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:17609131-Amino Acid Sequence, pubmed-meshheading:17609131-Aspartic Acid, pubmed-meshheading:17609131-Bacterial Proteins, pubmed-meshheading:17609131-Chemoreceptor Cells, pubmed-meshheading:17609131-Chemotaxis, pubmed-meshheading:17609131-Cytoplasm, pubmed-meshheading:17609131-Dose-Response Relationship, Drug, pubmed-meshheading:17609131-Escherichia coli, pubmed-meshheading:17609131-Escherichia coli Proteins, pubmed-meshheading:17609131-Molecular Sequence Data, pubmed-meshheading:17609131-Plasmids, pubmed-meshheading:17609131-Protein Conformation, pubmed-meshheading:17609131-Protein Engineering, pubmed-meshheading:17609131-Protein Kinases, pubmed-meshheading:17609131-Protein Structure, Tertiary, pubmed-meshheading:17609131-Receptors, Cell Surface, pubmed-meshheading:17609131-Recombinant Fusion Proteins, pubmed-meshheading:17609131-Sequence Homology, Amino Acid, pubmed-meshheading:17609131-Signal Transduction, pubmed-meshheading:17609131-beta-Galactosidase
pubmed:year
2007
pubmed:articleTitle
The design and development of Tar-EnvZ chimeric receptors.
pubmed:affiliation
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural