Control of Azospirillum brasilense NifA activity by PII:: effect of replacing Tyr residues of the NifA N-terminal domain on NifA activity

被引:22
作者
Arsène, F [1 ]
Kaminski, PA [1 ]
Elmerich, C [1 ]
机构
[1] Inst Pasteur, Dept Biotechnol, CNRS, Unite Physiol Cellulaire,URA D1300, F-75724 Paris 15, France
关键词
nitrogen fixation; NifA activity; glnB; Azospirillum brasilense;
D O I
10.1016/S0378-1097(99)00426-7
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
It was previously reported that the N-terminal domain of Azospirillum brasilense NifA was a negative regulator of the NifA activity and that the P-II protein prevented this inhibition under nitrogen fixing conditions, Here, we show that a mutation of a single Tyr residue at position 18 of the N-terminal domain of NifA led to an active NifA protein that did not require P-II for activation under nitrogen fixation conditions. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:339 / 343
页数:5
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