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Journal archive > 2012 > N 6 November-December

BIOINFORMATIC ANALYSIS OF POTENTIAL POST-TRANSLATIONAL MODIFICATION SITES
OF THE HUMAN O6-METHYLGUANINE-DNA METHYLTRANSFERASE (MGMT) PROTEIN

A. P. Iatsyshyna1, Z. M. Nidoieva2, O. V. Pidpala1, L. L. Lukash1

1Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv;
e-mail: This email address is being protected from spambots. You need JavaScript enabled to view it.;
2M. P. Drahomanov National Pedagogical University, Kyiv, Ukraine

Using in silico analysis a number of potential sites for post-translational modifications has been revealed within the human O6-methylguanine-DNA methyltransferase (MGMT) protein. In particular these were the acetylation of Gly3 residue in the N-terminus of protein and internal residues Lys132 and Lys135; Arg166 residue methy­lation; Lys63 SUMOylation and ubiquitination of Lys31, Lys39, Lys49, Lys63, Lys67, Lys135, Lys156, Lys196, Lys209. Also it has been predicted 16 novel potential phosphorylation sites of serine residues (positions 13, 124, 144, 182, 183, 190, 215, 216 and 230), tyrosine residues (positions 100 and 189) and threonine residues (positions 23, 69, 94, 126 and 229), as well as five binding sites for kinases and other proteins (Ser13 with 14-3-3, Val21 and Ile172 with D-domain, Pro78 and Pro111 with SH3-domain, Pro111 with MAPK3). Some kinases predicted by the authors are known as partners of the MGMT protein, that confirms the probability of modification of the given sites. Potential sites require further experimental confirmation of modi­fications and investigation of their influence on stability and DNA-repair activity of this protein.

Key words: O6-methylguanine-DNA methyltransferase (MGMT), post-translational protein modification, protein acetylation, protein methylation, protein SUMOylation, protein ubi­quitination, protein phosphorylation.

The original article in Ukrainian is available for download in PDF format.

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