TY  - JOUR
N1  - Copyright of this article belongs to Portland Press
ID  - open587
UR  - http://www.biochemj.org/bj/415/0027/4150027.pdf
IS  - 1
A1  - Thakur, Meghna
A1  - Chakraborti, Pradip K
Y1  - 2008/10/01/
N2  - Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we provide the evidence for the ability of PknA to transphosphorylate mMurD (mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate-ligase), the enzyme involved in peptidoglycan biosynthesis. Its co-expression in Escherichia coli along with PknA resulted in phosphorylation of mMurD. Consistent with these observations, results of the solid-phase binding assays revealed a high-affinity in vitro binding between the two proteins. Furthermore, overexpression of m-murD in Mycobacterium smegmatis yielded a phosphorylated protein. The results of the present study therefore point towards the possibility of mMurD being a substrate of PknA.
PB  - Portland Press
JF  - The Biochemical journal
VL  - 415
SN  - 1470-8728
TI  - Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis.
SP  - 27
AV  - restricted
EP  - 33
ER  -