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REVERSIBLE ADP-RIBOSYLATION AS A MECHANISM OF ENZYME REGULATION IN PROKARYOTES

被引：75
作者：
LUDDEN, PW
机构：
[1] Department of Biochemistry, University of Wisconsin, Madison, 53706, WI
来源：
MOLECULAR AND CELLULAR BIOCHEMISTRY | 1994年 / 138卷 / 1-2期
关键词：
ADP-RIBOSYLATION; NITROGEN FIXATION; NITROGENASE; DINITROGENASE REDUCTASE; PHOTOSYNTHETIC BACTERIA; NIF; DRA; GLUTAMINE SYNTHETASE; SIGNAL TRANSDUCTION;
D O I：
10.1007/BF00928453
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Several cases of ADP-ribosylation of endogenous proteins in procaryotes have been discovered and investigated. The most thoroughly studied example is the reversible ADP-ribosylation of the dinitrogenase reductase from the photosynthetic bacterium Rhodospirillum rubrum and related bacteria. A dinitrogenase reductase ADP-ribosyltransferase (DRAT) and a dinitrogenase reductase ADP-ribose glycohydrolase (DRAG) from R. rubrum have been isolated and characterized. The genes for these proteins have been isolated and sequences and show little similarity to the ADP-ribosylating toxins. Other targets for endogenous ADP-ribosylation by procaryotes include glutamine synthetase in R. rubrum and Rhizobium meliloti and undefined proteins in Streptomyces griseus and Pseudomonas maltophila.
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页码：123 / 129
页数：7
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