@article{mbs:/content/journal/micro/10.1099/mic.0.29171-0, author = "Xie, Zhihong and Dou, Yuetang and Ping, Shuzheng and Chen, Ming and Wang, Guoying and Elmerich, Claudine and Lin, Min", title = "Interaction between NifL and NifA in the nitrogen-fixing Pseudomonas stutzeri A1501", journal= "Microbiology", year = "2006", volume = "152", number = "12", pages = "3535-3542", doi = "https://doi.org/10.1099/mic.0.29171-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.29171-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "GST, glutathione S-transferase", 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.", }