Immunofluorescence microscopy using an IgG [alpha]-PknG-GST showed a lower abundance of PknG in the mycobacteria envelope of the wild type strain in stationary phase, as compared to the one registered during the exponential phase.
To evaluate the effect of the PknG C-terminal domain deletion on colony morphology, undiluted aliquots of 0, 4, 7, 14 and 21 days old cultures (Figure 4) of the wild type, mutant and complemented strains were grown on solid medium.
Dimerization of PknG and interaction with its substrate
The TPR domain is implicated in protein-protein interactions, and in PknG it has been shown to be involved in the formation of dimers during the crystallization of the protein (Scherr et al.
Comparative analysis of amino acid sequences of mycobacterial PknG proteins has shown that they have similar kinase, Trx and TPR domains (Houben et al.
In order to determine the role of the C-terminal domain TPR motif in the function of the PknG protein, a mutant of M.
tuberculosis lacking a complete PknG gene (Cowley et al.
As the deletion of the C-terminal domain of PknG leads to a decrease in the kinase activity (Tiwary et al.
However, since PknG had been previously proposed to interact with GarA through phosphothreonine residues located in the N-terminal domain of the protein (O'Hare et al.
The present results show that deletion of the C-terminal domain of the PknG protein of M.