MONO(ADP-RIBOSYLATION) IN RAT-LIVER MITOCHONDRIA
MONO(ADP-RIBOSYLATION) IN RAT-LIVER MITOCHONDRIA
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DOI：
10.1021/bi00402a004
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发表时间：
1988-01-26
期刊：
影响因子：
2.9
通讯作者：
RICHTER, C
中科院分区：
文献类型：
--
作者：
FREI, B;RICHTER, C
本文研究了大鼠肝线粒体中的蛋白质单（ADP-核糖基化）。在分离的线粒体内膜中，在ADP-核糖和NAD+两者的存在下，蛋白质以高特异性被单-（ADP-核糖基化）。该反应显然由酶促NAD+糖水解和随后游离ADP-核糖与受体蛋白的结合组成。在化学稳定性方面，所得键在迄今为止表征的ADP-核糖键中是独特的。游离ADP-核糖和受体蛋白之间的席夫碱加合物的形成被排除。在完整的线粒体中，至少有三类蛋白质在体内被ADP核糖基化。一个ADP-核糖-蛋白质键是羧酸酯型，如其在中性缓冲液中的不稳定性所示。另一类ADP-核糖基化蛋白质需要羟胺来释放ADP-核糖。第三类在羟胺中稳定，但对碱不稳定，类似于百日咳毒素形成的转导素中的ADP-核糖-半胱氨酸键。
This paper investigates protein mono(ADP-ribosylation) in rat liver mitochondria. In isolated inner mitochondrial membranes, in the presence of both ADP-ribose and NAD+, a protein is mono-(ADP-ribosylated) with high specificity. The reaction apparently consists of enzymatic NAD+ glycohydrolysis and subsequent binding of free ADP-ribose to the acceptor protein. In terms of chemical stability, the resulting bond is unique among the ADP-ribose linkages thus far characterized. Formation of a Schiff base adduct between free ADP-ribose and the acceptor protein is excluded. In intact mitochondria at least three classes of proteins are ADP-ribosylated in vivo. One ADP-ribose-protein linkage is of the carboxylate ester type as indicated by its lability in neutral buffer. Another class of ADP-ribosylated proteins requires hydroxylamine for release of ADP-ribose. The third class is stable in hydroxylamine but labile to alkali, similar to the ADP-ribose-cysteine linkage in transducin formed by pertussis toxin.