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Interactions between P II proteins and the nitrogenase regulatory enzymes DraT and DraG in Azospirillum brasilense
Author(s) -
Huergo Luciano F.,
Chubatsu Leda S.,
Souza Emanuel M.,
Pedrosa Fábio O.,
Steffens Maria B.R.,
Merrick Mike
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.054
Subject(s) - azospirillum brasilense , nitrogenase , enzyme , microbial inoculant , microbiology and biotechnology , drag , chemistry , biochemistry , biology , bacteria , physics , nitrogen fixation , genetics , thermodynamics
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 GlnZ 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.