Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases

BMC Genomics

Research

Nadezhda Yu Shashina¹  Alla I Yemets²  Alexey Yu Nyporko²  Yaroslav B Blume²  Vadym G Matusov²  Pavel A Karpov²  Elena S Nadezhdina³ 

[1] AN Belozersky Institute of Physical-Chemical Biology, Moscow State University, 119992, Leninsky GoryMoscow, Russian Federation;Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, 04123, Kyiv, Ukraine;Institute of Protein Research, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russian Federation;AN Belozersky Institute of Physical-Chemical Biology, Moscow State University, 119992, Leninsky GoryMoscow, Russian Federation;

关键词: Catalytic Domain;    PASK;    Protein Kinase Domain;    Plant Homologue;    Cell Division Regulation;   

DOI  :  10.1186/1471-2164-11-S1-S14

来源: Springer

【 摘 要 】

A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A number of SLK, MAST2 and AURKA plant homologues were identified. The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase). Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

【 授权许可】

Unknown   
© Karpov et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.