Sugawara Kiyoshi, Dohmae Naoshi, Kasai Koji, Saido-Sakanaka Hisako, Okamoto Susumu, Takio Koji, Ochi Kozo
National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan.
Biosci Biotechnol Biochem. 2002 Oct;66(10):2292-6. doi: 10.1271/bbb.66.2292.
An important role of protein ADP-ribosylation in bacterial morphogenesis has been proposed (J. Bacteriol. 178, 3785-3790; 178, 4935-4941). To clarify the detail of ADP-ribosylation, we identified a new kind of target protein for ADP-ribosylation in Streptomyces coelicolor A3(2) grown to the late growth phase. All four proteins (MalE, BldKB, a periplasmic protein for binding branched-chain amino-acids, and a periplasmic solute binding protein) were functionally similar and participated in the regulation of transport of metabolites or nutrients through the membrane. ADP-ribosylation was likely to occur on a cysteine residue, because the modification group was removed by mercuric chloride treatment. The modification site may be the site of lipoprotein modification necessary for protein export. This report is the first suggesting that certain proteins involved in membrane transport can be ADP-ribosylated.
蛋白质ADP-核糖基化在细菌形态发生中具有重要作用，这一观点已被提出（《细菌学杂志》178, 3785 - 3790；178, 4935 - 4941）。为了阐明ADP-核糖基化的细节，我们在生长至生长后期的天蓝色链霉菌A3(2)中鉴定出一种新型的ADP-核糖基化靶蛋白。所有四种蛋白质（麦芽糖结合蛋白、BldKB、一种用于结合支链氨基酸的周质蛋白以及一种周质溶质结合蛋白）在功能上相似，并且参与了代谢物或营养物质通过膜的运输调节。ADP-核糖基化可能发生在半胱氨酸残基上，因为修饰基团可通过氯化汞处理去除。修饰位点可能是蛋白质输出所需的脂蛋白修饰位点。本报告首次表明参与膜运输的某些蛋白质可被ADP-核糖基化。
