Mutational analysis of the structure basis for the multimerization function of NifA central domain

C Yang; G Yu; S Shen; J Zhu

doi:10.1007/BF02882072

Mutational analysis of the structure basis for the multimerization function of NifA central domain

Sci China C Life Sci. 2001 Feb;44(1):49-57. doi: 10.1007/BF02882072.

Authors

C Yang¹, G Yu, S Shen, J Zhu

Affiliation

¹ Laboratory of Molecular Genetics, Shanghai Institute of Plant Physiology, Chinese Academy of Sciences, 200032, Shanghai, China.

PMID: 18763088
DOI: 10.1007/BF02882072

Abstract

InKlebsiella pneumoniae (Kp) NifA central domain, when the conservative amino acid residue Thr-290 in C3 region was replaced by Val, the function of NifA for activating the transcription ofnif genes was lost. Thus the conservative Thr-290 residue seems critical for the activation function of NifA central domain. This point mutant of NifA central domain is used to examine the putative multimerization function of NifA central domain by merodiploid experiment. The results showed that the NifA central domain bore the multimerization determinants of NifA protein. A series of truncated mutants of NifA were constructed to determine the structural elements at the central domain critical for multimerization. It demonstrates that amino acid residues 252-453 are involved in the multimerization function of NifA central domain.