z-logo
open-access-imgOpen Access
Control of Azospirillum brasilense NifA activity by P II : effect of replacing Tyr residues of the NifA N‐terminal domain on NifA activity
Author(s) -
Arsène Florence,
Kaminski P.Alexandre,
Elmerich Claudine
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb08747.x
Subject(s) - regulator , residue (chemistry) , chemistry , nitrogen fixation , terminal (telecommunication) , azospirillum brasilense , domain (mathematical analysis) , biochemistry , nitrogen , gene , telecommunications , mathematical analysis , mathematics , organic chemistry , computer science
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here