In vitro distribution and characterization of membrane-associated PLD and PI-PLC in Brassica napus

被引:13
作者
Novotná, Z [1 ]
Martinec, J [1 ]
Profotová, B [1 ]
Zdárová, S [1 ]
Kader, JC [1 ]
Valentová, O [1 ]
机构
[1] Inst Chem Technol, Dept Biochem & Microbiol, Prague 16628 6, Czech Republic
关键词
Brassica napus; phospholipases; plasma membrane;
D O I
10.1093/jxb/erg070
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Two types of phosphollpid degrading enzyme, phospholipase D (PLD; EC 3.1.4.4) and phosphatyinositol-specific phospholipase C (PIP2-PLC; PI-PLC 3.1.4.11) were studied during the development of seeds and plants of Brassica napus. PLD exhibits two types of activity; polyphosphoinositide-requiring (PIP2-dependent PLD) and polyphosphoinositide-independent requiring millimolar concentrations of calcium (PLDalpha). Significantly different patterns of activity profiles were found for soluble and membrane-associated forms of all three enzymes within both processes. Membrane-associated PIP2-dependent PLD activity shows the opposite trend when compared to PLDalpha, while the highest PI-PLC activity appears in the same stages of development of seeds and plants as for PLDalpha. In subcellular fractions of hypocotyls of young plants, phospholipases were localized predominantly on plasma membranes. The biochemical characteristics (Ca2+, pH) of all three enzymes associated with plasma membrane vesicles, isolated by partitioning in an aqueous dextran-polyethylene glycol two-phase system, are also described. Direct interaction of PLDalpha with G-proteins under in vitro conditions was not confirmed.
引用
收藏
页码:691 / 698
页数:8
相关论文
共 23 条
[1]  
ARZ MC, 1994, PLANTA, V195, P57, DOI 10.1007/BF00206292
[2]  
Blatt MR, 2000, CURR OPIN PLANT BIOL, V3, P196, DOI 10.1016/S1369-5266(00)00064-9
[3]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[4]  
CRESPI P, 1993, ARCH SCI, V46, P335
[5]   NADH oxidase activity present on both the external and internal surfaces of soybean plasma membranes [J].
DeHahn, T ;
Barr, R ;
Morre, DJ .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1997, 1328 (02) :99-108
[6]   Subcellular distribution and tissue expression of phospholipase Dα, Dβ, and Dγ in Arabidopsis [J].
Fan, L ;
Zheng, SQ ;
Cui, DC ;
Wang, XM .
PLANT PHYSIOLOGY, 1999, 119 (04) :1371-1378
[7]  
LARSSON C, 1994, METHOD ENZYMOL, V228, P451
[8]   Cloning and direct G-protein regulation of phospholipase D from tobacco [J].
Lein, W ;
Saalbach, G .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, 2001, 1530 (2-3) :172-183
[9]   Subcellular localization of a high affinity binding site for D-myo-inositol 1,4,5-trisphosphate from Chenopodium rubrum [J].
Martinec, J ;
Feltl, T ;
Scanlon, CH ;
Lumsden, PJ ;
Machácková, I .
PLANT PHYSIOLOGY, 2000, 124 (01) :475-483
[10]   G protein activation stimulates phospholipase D signaling in plants [J].
Munnik, T ;
Arisz, SA ;
deVrije, T ;
Musgrave, A .
PLANT CELL, 1995, 7 (12) :2197-2210