Table of Contents
Computational Biology Journal
Volume 2014, Article ID 909268, 14 pages
http://dx.doi.org/10.1155/2014/909268
Research Article

Identification of Plant Homologues of Dual Specificity Yak1-Related Kinases

1Department of Genomics and Molecular Biotechnology, Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, Osipovskogo Street 2a, Kyiv 04123, Ukraine
2Department of General and Molecular Genetics, Taras Shevchenko National University of Kyiv (KNU), Glushkova Street 2, Kyiv 02090, Ukraine

Received 28 April 2014; Revised 16 September 2014; Accepted 25 September 2014; Published 8 December 2014

Academic Editor: Mihaly Mezei

Copyright © 2014 Pavel Karpov et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Currently, Dual Specificity YAK1-Related Kinases (MNB/DYRK) were found in slime molds, protista, fungi, and animals, but the existence of plant homologues is still unclear. In the present study, we have identified 14 potential plant homologues with the previously unknown functions, based on the strong sequence similarity. The results of bioinformatics analysis revealed their correspondence to DYRK1A, DYRK1B, DYRK3, and DYRK4. For two plant homologues of animal DYRK1A from Physcomitrella patens and Arabidopsis thaliana spatial structures of catalytic domains were predicted, as well as their complexes with ADP and selective inhibitor d15. Comparative analysis of 3D-structures of the human DYRK1A and plant homologues, their complexes with the specific inhibitors, and results of molecular dynamics confirm their structural and functional similarity with high probability. Preliminary data indicate the presence of potential MNB/DYRK specific phosphorylation sites in such proteins associated with plant cytoskeleton as plant microtubule-associated proteins WVD2 and WDL1, and FH5 and SCAR2 involved in the organization and polarity of the actin cytoskeleton and some kinesin-like microtubule motor proteins.