Expression, purification, and functional analysis of the C-terminal domain of Herbaspirillum seropedicae NifA protein

2003 ◽  
Vol 27 (2) ◽  
pp. 313-318 ◽  
Author(s):  
Rose A Monteiro ◽  
Emanuel M Souza ◽  
M Geoffrey Yates ◽  
M.Berenice R Steffens ◽  
Fábio O Pedrosa ◽  
...  
2010 ◽  
Vol 19 (5) ◽  
pp. 974-986 ◽  
Author(s):  
Mengmeng Zhang ◽  
June Liu ◽  
Youngjun Kim ◽  
Jack E. Dixon ◽  
Samuel L. Pfaff ◽  
...  

2000 ◽  
Vol 46 (11) ◽  
pp. 1087-1090 ◽  
Author(s):  
Rose A. Monteiro ◽  
Emanuel M. Souza ◽  
M. Geoffrey Yates ◽  
Fábio O. Pedrosa ◽  
Leda S. Chubatsu

1999 ◽  
Vol 258 (2) ◽  
pp. 366-373 ◽  
Author(s):  
Ren-He Xu ◽  
Robert J. Lechleider ◽  
Hsiu-Ming Shih ◽  
Chen-Fei Hao ◽  
Dvora Sredni ◽  
...  

FEBS Letters ◽  
1999 ◽  
Vol 447 (2-3) ◽  
pp. 283-286 ◽  
Author(s):  
R.A Monteiro ◽  
E.M Souza ◽  
S Funayama ◽  
M.G Yates ◽  
F.O Pedrosa ◽  
...  

1999 ◽  
Vol 180 (2) ◽  
pp. 157-161 ◽  
Author(s):  
Rose Adele Monteiro ◽  
Emanuel M Souza ◽  
M.Geoffrey Yates ◽  
Fábio O Pedrosa ◽  
Leda S Chubatsu
Keyword(s):  

2003 ◽  
Vol 69 (3) ◽  
pp. 1527-1531 ◽  
Author(s):  
Rose A. Monteiro ◽  
Emanuel M. de Souza ◽  
M. Geoffrey Yates ◽  
Fabio O. Pedrosa ◽  
Leda S. Chubatsu

ABSTRACT Herbaspirillum seropedicae is an endophytic diazotroph belonging to the β-subclass of the class Proteobacteria, which colonizes many members of the Gramineae. The activity of the NifA protein, a transcriptional activator of nif genes in H. seropedicae, is controlled by ammonium ions through its N-terminal domain and by oxygen through mechanisms that are not well understood. Here we report that the NifA protein of H. seropedicae is inactive and more susceptible to degradation in an fnr Escherichia coli background. Both effects correlate with oxygen exposure and iron deprivation. Our results suggest that the oxygen sensitivity and iron requirement for H. seropedicae NifA activity involve the Fnr protein.


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