Open AccessInteraction between NifL and NifA in the nitrogen-fixing Pseudomonas stutzeri A1501
Author(s) -
Zhihong Xie,
Yuetang Dou,
Shuzheng Ping,
Ming Chen,
Guoying Wang,
Claudine Elmerich,
Min Lin
Publication year - 2006
Publication title -
microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 179
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/mic.0.29171-0
Subject(s) - pseudomonas stutzeri , nitrogenase , complementation , mutant , microbiology and biotechnology , chemistry , biology , biochemistry , nitrogen fixation , bacteria , genetics , gene
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.