Interactions between PII proteins and the nitrogenase regulatory enzymes DraT and DraG in Azospirillum brasilense

被引:40
作者
Huergo, Luciano F.
Chubatsu, Leda S.
Souza, Emanuel M.
Pedrosa, Fabio O.
Steffens, Maria B. R.
Merrick, Mike [1 ]
机构
[1] John Innes Ctr Plant Sci Res, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England
[2] Univ Fed Parana, Dept Biochem & Mol Biol, BR-81531990 Curitiba, Parana, Brazil
基金
英国生物技术与生命科学研究理事会;
关键词
ADP-ribosylation; nitrogenase; DraT; DraG; P-II protein; REDUCTASE-ACTIVATING GLYCOHYDROLASE; RHODOSPIRILLUM-RUBRUM; FUNCTIONAL-CHARACTERIZATION; DINITROGENASE REDUCTASE; ADP-RIBOSYLATION; MEMBRANE SEQUESTRATION; OVER-EXPRESSION; SWITCH-OFF; AMMONIUM; GLNB;
D O I
10.1016/j.febslet.2006.08.054
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In Azospirillum brasilense. ADP-ribosylation of dinitrogenase reductase (NifH) occurs in response to addition of ammonium to the extracellular medium and is mediated by dinitrogenase reductase ADP-ribosyltransferase (DraT) and reversed by dinitrogenase reductase glycohydrolase (DraG). The P-II proteins GlnB and GluZ have been implicated in regulation of DraT and DraG by an as yet unknown mechanism. Using pull-down experiments with His-tagged versions of DraT and DraG we have now shown that DraT binds to GlnB, but only to the deuridylylated form, and that DraG binds to both the uridylylated and deuridylylated forms of GlnZ. The demonstration of these specific protein complexes, together with our recent report of the ability of deuridylylated GlnZ to be sequestered to the cell membrane by the ammonia channel protein AmtB, offers new insights into the control of NifH ADP-ribosylation. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:5232 / 5236
页数:5
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