Symbionin, a GroEL homologous molecular chaperone produced by an intracellular symbiont of the pea aphid, is autocatalytically phosphorylated in vitro at elevated temperatures. The phosphorylated symbionin showed a potent suppressive activity in spontaneous refolding of chemically denatured dihydrofolate reductase. When the 32P-labeled autophosphorylated symbionin was incubated with ADP, a portion of the radioactivity was transferred to ADP, suggesting that the autocatalytically phosphorylated symbionin contains high-energy phosphate bonds. It was also shown that when symbionin was incubated with [gamma-32P]ATP and GDP, a large amount of the radioactivity was found in GTP, indicating that phosphate transfer between ATP and GDP is catalyzed by symbionin. These results suggested that in the endosymbiotic system symbionin functions as not only a molecular chaperone but also an energy-coupling protein.
Chaperonin produced by an intracellular symbiont is an energy-coupling protein with phosphotransferase activity. Publishing Authors By Initials
Chaperonin produced by an intracellular symbiont is an energy-coupling protein with phosphotransferase activity. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Journal of biochemistry
VOLUME: 114
Page Numbers: 246-50
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: Aug
YEAR: 1993
Chaperonin produced by an intracellular symbiont is an energy-coupling protein with phosphotransferase activity. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 376600
Chaperonin produced by an intracellular symbiont is an energy-coupling protein with phosphotransferase activity. Keywords Mesh Terms:
KEYWORDS: Proteins
MESH TERMS: metabolism
Chemical & Substance for Abstract: Chaperonin produced by an intracellular symbiont is an energy-coupling protein with phosphotransferase activity. Information
Substance Name: Phosphotransferases
Registry Number: EC 2.7.-
Grant and Affiliation Information for Chaperonin produced by an intracellular symbiont is an energy-coupling protein with phosphotransferase activity.
AFFILIATION: Zoological Institute, Faculty of Science, University of Tokyo.
Country: JAPAN
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MEDLINETA: J Biochem
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