XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

Posters
72.
BIOCHEMICal CHaraCTErIZaTION of Rv1459c prOTEIN PUTaTIve
GT-C GLYCOSYLTraNSferaSE frOM MYCOBaCTEria
Milo Bystrický 1 , Martina Beláňová 1 , Mary Jackson 2 ,
Katarína Mikušová 1 and Jana Korduláková 1
1
Department of Biochemistry, Faculty of Natural Sciences, Comenius University,
Bratislava, Slovakia; 2 Department of Microbiology, Immunology, and Pathology,
Colorado State University, Fort Collins, CO, USA
Mycobacterium tuberculosis and related species of the order Actinomycetales carry
a significant number of glycosyltransferases of the GT-C class. This group of glycosyltransferases
comprises integral membrane proteins with dependency on polyprenylphosphate-linked
sugar donors. No protein structure of the GT-C superfamily has yet
been solved. In mycobacteria GT-C glycosyltransferases are believed to be involved in
the later biosynthetic steps of key polysaccharides in the mycobacterial cell envelope.
We focused on the functional characterization of the mycobacterial protein Rv1459c,
putative GT-C glycosyltransferase encoded by the gene located in the cluster of the
genes rv1459c-rv1456c. Homologues of the genes rv1459c - rv1456c are present in all
mycobacterial species sequenced so far. Similar gene clusters were identified also in
corynebacteria and nocardia - organisms with the cell wall structures very similar to that
of mycobacteria. The glycosyltransferase Rv1459c was produced in E. coli in the form
of soluble protein fused with the maltose binding protein. Heterologous production of
the soluble Rv1459c allowed us to isolate this protein for crystallography purposes, as
well as for the investigation of the interactions between Rv1459c and the subunits of
the ABC transporter Rv1458c/Rv1457c/Rv1456c.
Acknowledgement: This work was supported by Slovak Research and Development
Agency (grant No. APVV-0499-07)
XXII. Biochemistry Congress, Martin
195