Molecular characterization of a tyrosine-specific protein phosphatase encoded by a stress-responsive gene in Arabidopsis

被引:134
作者
Xu, Q [1 ]
Fu, HH [1 ]
Gupta, R [1 ]
Luan, S [1 ]
机构
[1] Univ Calif Berkeley, Dept Plant & Microbial Biol, Berkeley, CA 94720 USA
关键词
D O I
10.1105/tpc.10.5.849
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein tyrosine kinases and phosphatases play a vital role in the regulation of cell growth and differentiation in animal systems. However, none of these enzymes has been characterized from higher plants. In this study, we isolated a cDNA encoding a putative protein tyrosine phosphatase (PTPase) from Arabidopsis (referred to as AtPTP1). The expression level of AtPTP1 is highly sensitive to environmental stresses. High-salt conditions increased AtPTP1 mRNA levels, whereas cold treatment rapidly eliminated the AtPTP1 transcript. The recombinant AtPTP1 protein specifically hydrolyzed phosphotyrosine, but not phosphoserine/threonine, in protein substrates. Site-directed mutagenesis defined two highly conserved amino acids, cysteine-265 and aspartate-234, as being essential for the phosphatase activity of the AtPTP1 protein, suggesting a common catalytic mechanism for PTPases from all eukaryotic systems. In summary, we have identified AtPTP1 as a tyrosine-specific protein phosphatase that may function in stress responses of higher plants.
引用
收藏
页码:849 / 857
页数:9
相关论文
共 52 条
[51]   Salicylic acid activates a 48-kD MAP kinase in tobacco [J].
Zhang, SQ ;
Klessig, DF .
PLANT CELL, 1997, 9 (05) :809-824
[52]   DISSECTING THE CATALYTIC MECHANISM OF PROTEIN-TYROSINE PHOSPHATASES [J].
ZHANG, ZY ;
WANG, YA ;
DIXON, JE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (05) :1624-1627