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Microbiology 152 (2006), 3535-3542; DOI  10.1099/mic.0.29171-0
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Microbiology 152 (2006), 3535-3542; DOI  10.1099/mic.0.29171-0
© 2006 Society for General Microbiology

Interaction between NifL and NifA in the nitrogen-fixing Pseudomonas stutzeri A1501

Zhihong Xie1,{dagger}, Yuetang Dou1, Shuzheng Ping1, Ming Chen1, Guoying Wang2, Claudine Elmerich3,{ddagger} and Min Lin1

1 Biotechnology Research Institute, CAAS, Beijing, PR China
2 Biology College, China Agricultural University, Beijing, PR China
3 Institut des Sciences du Végétal, CNRS UPR-2355, Gif-sur-Yvette, France

Correspondence
Min Lin
linmin57{at}vip.163.com

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.

Abbreviations: GST, glutathione S-transferase

{dagger}Present address: Department of Biochemistry, Cellular and Molecular Biology, the University of Tennessee, Knoxville, TN 37996, USA.

{ddagger}Present address: Département de Microbiologie, Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, 75724 Paris Cedex 15, France.




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