Biochemical and physiological characterization of the GTP-binding protein Obg of Mycobacterium tuberculosis.

ABSTRACT:

Background

Obg is a highly conserved GTP-binding protein that has homologues in bacteria, archaea and eukaryotes. In bacteria, Obg proteins are essential for growth, and they participate in spore formation, stress adaptation, ribosome assembly and chromosomal partitioning. This study was undertaken to investigate the biochemical and physiological characteristics of Obg in Mycobacterium tuberculosis, which causes tuberculosis in humans.

Results

We overexpressed M. tuberculosis Obg in Escherichia coli and then purified the protein. This protein binds to, hydrolyzes and is phosphorylated with GTP. An anti-Obg antiserum, raised against the purified Obg, detects a 55 kDa protein in immunoblots of M. tuberculosis extracts. Immunoblotting also discloses that cultured M. tuberculosi

SUBMITTER: Sasindran SJ 

PROVIDER: S-EPMC3056739 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature