Linked Life Data

7896735

Source:http://linkedlifedata.com/resource/pubmed/id/7896735

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-4-26
pubmed:abstractText
Symbionin, a GroEL homologous molecular chaperone produced by an intracellular symbiont of the pea aphid, is able to transfer its high-energy phosphate bond to other compounds through its autophosphorylation. When the urea-dissociated monomeric symbionin fixed onto a polyvinylidene difluoride membrane was incubated with [gamma-32P] ATP, it was efficiently phosphorylated at elevated temperatures. The autophosphorylated monomeric 32P-labeled symbionin, when incubated with ADP, transferred a significant portion of its radioactivity to ADP, suggesting that the autocatalytically phosphorylated monomeric symbionin contains high-energy phosphate bonds. It was also shown that when symbiotic proteins were electrophoretically separated, blotted onto a polyvinylidene disulfide membrane and incubated with 32P-labeled symbionin, radioactivity was found on several kinds of polypeptides, indicating that the phosphoryl group was transferred from symbionin to other symbiotic proteins. Peptide sequence analysis and thin-layer chromatographic analysis of the 32P-labeled tryptic fragment of the phosphorylated symbionin revealed that the site of phosphorylation is His-133. These results suggested that symbionin functions as a histidine protein kinase, or a sensor molecule, of the two-component pathway known in other organisms. However, symbionin is not similar in amino acid sequence to any known histidine protein kinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
116
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1075-81
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
An endosymbiont chaperonin is a novel type of histidine protein kinase.
pubmed:affiliation
Zoological Institute, Graduate School of Science, University of Tokyo.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't