Protein kinase I of Mycobacterium tuberculosis: cellular localization and expression during infection of macrophage-like cells.
Protein kinase I of Mycobacterium tuberculosis, which has an unusual amino acid composition in its catalytic loop, displayed autophosphorylation and transphosphorylation activity. Immunoblot analysis of sub-cellular fractions of M. tuberculosis, using anti-PknI antibodies raised in rabbits, showed that PknI localizes to the bacterial cytosol. In contrast, PknA was membrane-bound. Relative expression of pknI, when measured by combining molecular beacons and RT-PCR, decreased during infection of THP-1 human macrophages. Expression of pknA and pknB was upregulated during infection. Thus PknI represents a group of protein kinases that is distinct from the more extensively studied enzymes PknA and PknB.
Singh
Anubha
A
Public Health Research Institute, 225 Warren Street, Newark, NJ 07103, USA.
Singh
Yogendra
Y
Pine
Richard
R
Shi
Lanbo
L
Chandra
Ramesh
R
Drlica
Karl
K
D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D008264:Macrophages / Q000382:microbiology; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D051057:Proto-Oncogene Proteins c-akt / Q000378:metabolism; D011817:Rabbits; D015533:Transcriptional Activation
D001426:Bacterial Proteins; D011494:Protein Kinases; D051057:Proto-Oncogene Proteins c-akt; D017868:Cyclic AMP-Dependent Protein Kinases