Cloning and characterization of engA, a GTP-binding protein from Mycobacterium tuberculosis H(37)Rv.

Guanine nucleotides are key signaling molecules and many members of the G-protein family bind and hydrolyze nucleotides, particularly GTP, and regulate intracellular level of GTP and GDP. EngA is one of the members of these universally conserved GTPases. Amino acid sequence alignment of EngA of Mycobacterium tuberculosis H(37)Rv with other homologous bacterial proteins have shown that EngA of M. tuberculosis H(37)Rv has significant homology with EngA of other bacteria. EngA protein has shown GTP-binding and GTP hydrolysis activities as intrinsic biochemical properties of protein and this serves as a base to further investigate the physiological significance of this protein in the pathogenesis mechanism of M. tuberculosis H(37)Rv. In this paper for the first time EngA GTP-binding protein of M. tuberculosis H(37)Rv was functionally characterized for its GTPase and GTP-hydrolyzing activity. GTPases such as era, obg, lepA, and FtsZ are vital for growth and development and specifically cellular functions of bacteria, in view of these observations it can be concluded that EngA GTPase can be further utilized for the study of its functional role in the pathogenesis of M. tuberculosis H(37)Rv.