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首页> 外文期刊>Journal of bacteriology >ADP-Ribosylation of Variants of Azotobacter vinelandiiDinitrogenase Reductase by Rhodospirillum rubrumDinitrogenase Reductase ADP-Ribosyltransferase
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ADP-Ribosylation of Variants of Azotobacter vinelandiiDinitrogenase Reductase by Rhodospirillum rubrumDinitrogenase Reductase ADP-Ribosyltransferase

机译：红螺螺旋螺旋菌对藤蔓固氮菌双亚硝基酶还原酶变体的ADP-核糖基化作用ADP-核糖基转移酶

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In a number of nitrogen-fixing bacteria, nitrogenase is posttranslationally regulated by reversible ADP-ribosylation of dinitrogenase reductase. The structure of the dinitrogenase reductase from Azotobacter vinelandii is known. In this study, mutant forms of dinitrogenase reductase from A. vinelandii that are affected in various protein activities were tested for their ability to be ADP-ribosylated or to form a complex with dinitrogenase reductase ADP-ribosyltransferase (DRAT) fromRhodospirillum rubrum. R140Q dinitrogenase reductase could not be ADP-ribosylated by DRAT, although it still formed a cross-linkable complex with DRAT. Thus, the Arg 140 residue of dinitrogenase reductase plays a critical role in the ADP-ribosylation reaction. Conformational changes in dinitrogenase reductase induced by an F135Y substitution or by removal of the Fe4S4 cluster resulted in dinitrogenase reductase not being a substrate for ADP-ribosylation. Through cross-linking studies it was also shown that these changes decreased the ability of dinitrogenase reductase to form a cross-linkable complex with DRAT. Substitution of D129E or deletion of Leu 127, which result in altered nucleotide binding regions of these dinitrogenase reductases, did not significantly change the interaction between dinitrogenase reductase and DRAT. Previous results showed that changing Lys 143 to Gln decreased the binding between dinitrogenase reductase and dinitrogenase (L. C. Seefeldt, Protein Sci. 3:2073–2081, 1994); however, this change did not have a substantial effect on the interaction between dinitrogenase reductase and DRAT.
机译：在许多固氮细菌中，固氮酶受二氮酶还原酶可逆的ADP-核糖基化作用的翻译后调控。葡萄固氮杆菌的双氮酶还原酶的结构是已知的。在这项研究中，来自 A的二硝基酶还原酶的突变形式。对受各种蛋白质活性影响的藤蔓进行了ADP核糖基化处理或与来自红螺螺旋藻的双氮还原酶ADP核糖基转移酶（DRAT）形成复合物的能力进行了测试。尽管R140Q双氮酶还原酶仍与DRAT形成可交联的复合物，但它不能被DRAT进行ADP核糖基化。因此，双氮还原酶的Arg 140残基在ADP-核糖基化反应中起关键作用。 F135Y取代或除去Fe 4 S 4 团簇引起的二氧化氮还原酶的构象变化导致二氧化氮还原酶不是ADP-核糖基化的底物。通过交联研究，还表明这些变化降低了二硝基酶还原酶与DRAT形成可交联复合物的能力。 D129E的取代或Leu 127的缺失（导致这些双氮酶还原酶的核苷酸结合区域发生改变）并没有显着改变双氮酶还原酶与DRAT之间的相互作用。先前的结果表明，将Lys 143更改为Gln会降低二氧化氮还原酶和二氧化氮之间的结合（L. C. Seefeldt，Protein Sci。3：2073–2081，1994）;但是，这种变化对二氮还原酶与DRAT之间的相互作用没有实质性影响。

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