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Journal of Bacteriology, August 2006, p. 6020-6025, Vol. 188, No. 16
0021-9193/06/$08.00+0     doi:10.1128/JB.00379-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Peptidyl-Prolyl cis/trans Isomerase-Independent Functional NifH Mutant of Azotobacter vinelandii{dagger}

Nara Gavini,* Sudheer Tungtur, and Lakshmi Pulakat

Department of Biological Sciences, Mississippi State University, Mississippi State, Mississippi 39762

Received 16 March 2006/ Accepted 25 May 2006

Peptidyl-prolyl cis/trans isomerases (PPIases) play a pivotal role in catalyzing the correct folding of many prokaryotic and eukaryotic proteins that are implicated in a variety of biological functions, ranging from cell cycle regulation to bacterial infection. The nif accessory protein NifM, which is essential for the biogenesis of a functional NifH component of nitrogenase, is a PPIase. To understand the nature of the molecular signature that defines the NifM dependence of NifH, we screened a library of nifH mutants in the nitrogen-fixing bacterium Azotobacter vinelandii for mutants that acquired NifM independence. Here, we report that NifH can acquire NifM independence when the conserved Pro258 located in the C-terminal region of NifH, which wraps around the other subunit in the NifH dimer, is replaced by serine.

* Corresponding author. Mailing address: Department of Biological Sciences, P.O. Box GY, Mississippi State University, Mississippi State, MS 39762. Phone: (662) 325-7573. Fax: (662) 325-7939. E-mail: gavini{at}biology.msstate.edu.

{dagger} Dedicated to the memory of the late Barbara K. Burgess, of the University of California at Irvine, who strove to improve the lives of foreign and female students.

Journal of Bacteriology, August 2006, p. 6020-6025, Vol. 188, No. 16
0021-9193/06/$08.00+0     doi:10.1128/JB.00379-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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