Control of Azospirillum brasilense NifA activity by P(II): effect of replacing Tyr residues of the NifA N-terminal domain on NifA activity.
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.
Arsène
F
F
Unité de Physiologie Cellulaire, Centre National de la Recherche Scientifique URA D1300, Département des Biotechnologies, Institut Pasteur, 25 rue du Docteur Roux, 75724, Paris, France.
Kaminski
P A
PA
Elmerich
C
C
D000595:Amino Acid Sequence; D015806:Azospirillum brasilense / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology*; D001483:Base Sequence; D008969:Molecular Sequence Data; D009586:Nitrogen Fixation; D051922:PII Nitrogen Regulatory Proteins; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000737:chemistry / Q000502:physiology*
D001426:Bacterial Proteins; C061338:NifA protein, Bacteria; D051922:PII Nitrogen Regulatory Proteins; D014157:Transcription Factors; C404143:PIID regulatory protein, Bacteria