CHOLINE OXIDASE, A CATABOLIC ENZYME IN ARTHROBACTER-PASCENS, FACILITATES ADAPTATION TO OSMOTIC-STRESS IN ESCHERICHIA-COLI

被引:64
作者
ROZWADOWSKI, KL
KHACHATOURIANS, GG
SELVARAJ, G
机构
[1] NATL RES COUNCIL CANADA, INST PLANT BIOTECHNOL, SASKATOON S7N 0W9, SASKATCHEWAN, CANADA
[2] UNIV SASKATCHEWAN, DEPT APPL MICROBIOL & FOOD SCI, SASKATOON S7N 0W0, SASKATCHEWAN, CANADA
关键词
D O I
10.1128/jb.173.2.472-478.1991
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Choline oxidase (EC 1.1.3.17) is a bifunctional enzyme that is capable of catalyzing glycine betaine biosynthesis from choline via betaine aldehyde. A gene (cox) encoding this enzyme in the gram-positive soil bacterium Arthrobacter pascens was isolated and characterized. This gene is contained within a 1.9-kb fragment that encodes a polypeptide of approximately 66 kDa. Transfer of this gene to an Escherichia coli mutant that is defective in betaine biosynthesis resulted in an osmotolerant phenotype. This phenotype was associated with the ability of the host to synthesize and assemble an enzymatically active choline oxidase that could catalyze biosynthesis of glycine betaine from an exogenous supply of chlorine. Although glycine betaine functions as an osmolyte in several different organisms, it was not found to have this role in A. pascens. Instead, both choline and glycine betaine were utilized as carbon sources. In A. pascens synthesis and activity of choline oxidase were modulated by carbon sources and were susceptible to catabolite repression. Thus, cox, a gene concerned with carbon utilization in A. pascens, was found to play a role in adaptation to an environmental stress in a heterologous organism. In addition ot providing a possible means of manipulating osmotolerance in other organisms, the cox gene offers a model system for the study of choline oxidation, an important metabolic process in both procaryotes and eucaryotes.
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页码:472 / 478
页数:7
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