Identification of the diacylglycerol kinase structural gene of Rhizobium meliloti 1021.
Mol Plant Microbe Interact
; 5(5): 363-71, 1992.
Article
en En
| MEDLINE
| ID: mdl-1335301
ABSTRACT
The cyclic beta-1,2-glucans of Rhizobium may function during legume nodulation. These molecules may become highly substituted with phosphoglycerol moieties from the head group of phosphatidylglycerol; diglyceride is a by-product of this reaction (K. J. Miller, R. S. Gore, and A. J. Benesi, J. Bacteriol. 1704569-4575, 1988). We recently reported that R. meliloti 1021 produces a diacylglycerol kinase (EC 2.7.1.107) activity that shares several properties with the diacylglycerol kinase enzyme of Escherichia coli (W. P. Hunt, R. S. Gore, K. J. Miller, Appl. Environ. Microbiol. 573645-3647, 1991). A primary function of this rhizobial enzyme is to recycle diglyceride generated during cyclic beta-1,2-glucan biosynthesis. In the present study, we report the cloning and initial characterization of a single-copy gene from R. meliloti 1021 that encodes a diacylglycerol kinase homolog; this homolog can complement a diacylglycerol kinase deficient strain of E. coli. The sequence of the rhizobial diacylglycerol kinase gene was predicted to encode a protein of 137 amino acids; this protein shares 32% identity with the E. coli enzyme. Analysis of hydropathy and the potential to form specific secondary structures indicated a common overall structure for the two enzymes. Because diglyceride metabolism and cyclic beta-1,2-glucan biosynthesis are metabolically linked, future studies with diacylglycerol kinase mutants of R. meliloti 1021 should further elucidate the roles of the cyclic beta-1,2-glucans in the Rhizobium-legume symbiosis.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfotransferasas
/
Sinorhizobium meliloti
Tipo de estudio:
Diagnostic_studies
Idioma:
En
Revista:
Mol Plant Microbe Interact
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BOTANICA
/
MICROBIOLOGIA
Año:
1992
Tipo del documento:
Article