Abstract
Using yeast two-hybrid assay, we investigated protein-protein
interactions between all orthologous histidine kinase
(HK)/response regulator (RR) pairs of M. tuberculosis H37Rv
and identified potential protein-protein interactions between
a noncognate HK/RR pair, DosT/NarL. The protein
interaction between DosT and NarL was verified by phosphotransfer
reaction from DosT to NarL. Furthermore, we
found that the DosT and DosS HKs, which share considerable
sequence similarities to each other and form a twocomponent
system with the DosR RR, have different crossinteraction
capabilities with NarL: DosT interacted with
NarL, while DosS did not. The dimerization domains of
DosT and DosS were shown to be sufficient to confer specificity
for DosR, and the different cross-interaction abilities
of DosS and DosT with NarL were demonstrated to be attributable
to variations in the amino acid sequences of the
α2-helices of their dimerization domains.
Citations
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