Expression and characterization of Arabidopsis phospholipase Dγ2

被引:16
作者
Qin, Chunbo
Li, Maoyin
Qin, Wensheng
Bahn, Sung Chul
Wang, Cunxi
Wang, Xuemin
机构
[1] Univ Missouri, Dept Biol, St Louis, MO 63121 USA
[2] Donald Danforth Plant Sci Ctr, St Louis, MO 63132 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2006年 / 1761卷 / 12期
基金
美国国家科学基金会;
关键词
Arabidopsis; phospholipase D; phospholipid hydrolysis; gene expression; substrate composition; membrane environment;
D O I
10.1016/j.bbalip.2006.09.017
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
The phospholipase D (PLD) family of Arabidopsis thaliana has 12 identified members, including three highly homologous PLD gamma s. The enzymatic and molecular properties of PLD gamma 2 were characterized and compared with those of PLD gamma 1. Two variants of PLD gamma 2 cDNAs, designated PLD gamma 2a and PLD gamma 2b, were isolated, and they differ in the presence of a 96-nucleotide fragment at the beginning of the open reading frame. Catalytically active PLD gamma 2a was expressed in E. coli. PLD gamma 2a and gamma 1 both require phosphatidylinositol 4,5-bisphosphate (PIP2) and calcium for activity, but they differ in the effect Of PIP2 and Triton X-100 on their activities. While Triton X-100 could greatly activate PLD gamma 1 activity and served only as a neutral diluent in the substrate vesicles, it totally abolished PLD-gamma 2a activity and prohibited any stimulation effect from PIP2. PLD gamma 2a misses one of the basic, PIP2-interacting residues, which may weaken the binding of PIP2 to PLD gamma 2a. In addition, PLD gamma 2 and PLD gamma 1 displayed different patterns of expression in different tissues, and the transcript of PLD gamma 2a differs from that of PLD gamma 1 by having a longer 5'-UTR. These differences in biochemical and molecular properties suggest that the highly homologous PLD gamma s are subjected to unique regulations and might have distinguishable functions. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1450 / 1458
页数:9
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