Functional Analysis of a type-2C Protein Phosphatase (AtPP2C52) in Arabidopsis thaliana  

Hua Liu1 , Daisuke Tsugama1 , Shenkui Liu2 , Tetsuo Takano1
1 Asian Natural Environmental Science Center (ANESC), The University of Tokyo, Tokyo 188-0002, Japan
2 Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin 150040, PR China
1 Asian Natural Environmental Science Center (ANESC), The University of Tokyo, Tokyo 188-0002, Japan
2 Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin 150040, PR China
1 Asian Natural Environmental Science Center (ANESC), The University of Tokyo, Tokyo 188-0002, Japan
2 Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin 150040, PR China
Author    Correspondence author
Genomics and Applied Biology, 2013, Vol. 4, No. 1   doi: 10.5376/gab.2013.04.0001
Received: 18 Dec., 2012    Accepted: 24 Dec., 2012    Published: 30 Jan., 2013
© 2013 BioPublisher Publishing Platform
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

 Liu et al., 2013, Functional analysis of a type-2C protein phosphatase (AtPP2C52) in Arabidopsis thaliana, Genomics and Applied Biology, 2013, Vol.4 No.1 1-7 (doi: 10.3969/gab.2013.04.0001)

Abstract

AtPP2C52 is a plasma membrane type-2C protein phosphatase. In this study, AtPP2C52 promoter-GUS analysis revealed that AtPP2C52 gene was found in a broad expression spectrum with a higher level in the vascular and meristem. AtPP2C52 can interact with multiple proteins, including a proteasome maturation factor, UMP1, and a cysteine proteinase, RD21a, as well as the heterotrimeric G proteins β subunit, AGB1. By mutational analysis of AtPP2C52, it was identified that some residues were essential for AtPP2C52 to bind AGB1, UMP1 and RD21a, suggesting that these proteins should be potential substrates of AtPP2C52.

Keywords
Protein phosphatase; Vascular; Protein-protein interaction; Arabidopsis thaliana
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