Interaction between NifL and NifA in the nitrogen-fixing Pseudomonas stutzeri A1501
Xie, Zhihong and Dou, Yuetang and Ping, Shuzheng and Chen, Ming and Wang, Guoying and Elmerich, Claudine and Lin, Min,, 152, 3535-3542 (2006),
doi = https://doi.org/10.1099/mic.0.29171-0,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= Pseudomonas stutzeri strain A1501 isolated from rice fixes nitrogen under microaerobic conditions in the free-living state. This paper describes the properties of nifL and nifA mutants as well as the physical interaction between NifL and NifA proteins. A nifL mutant strain that carried a mutation non-polar on nifA expression retained nitrogenase activity. Complementation with a plasmid containing only nifL led to a decrease in nitrogenase activity in both the wild-type and the nifL mutant, suggesting that NifL acts as an antiactivator of NifA activity. Using the yeast two-hybrid system and purified protein domains of NifA and NifL, an interaction was shown between the C-terminal domain of NifL and the central domain of NifA, suggesting that NifL antiactivator activity is mediated by direct protein interaction with NifA.,
language=,
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