pH and carbon supply control the expression of phosphoenolpyruvate carboxylase kinase genes in Arabidopsis thaliana

被引:19
作者
Chen, Zhi-Hui [1 ]
Jenkins, Gareth I. [1 ]
Nimmo, Hugh G. [1 ]
机构
[1] Univ Glasgow, Div Mol & Cellular Biol, Fac Biomed & Life Sci, Glasgow G12 8QQ, Lanark, Scotland
基金
英国生物技术与生命科学研究理事会;
关键词
intracellular pH; nitrogen supply; phosphoenolpyruvate carboxykinase; protein phosphorylation;
D O I
10.1111/j.1365-3040.2008.01885.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Phosphoenolpyruvate carboxylase (PEPC) is thought to play many roles in C-3 plants including the provision of biosynthetic precursors and control of pH during N assimilation. Its activity is controlled via phosphorylation catalysed by PEPC kinases, which are encoded by PPCK genes. We examined PPCK expression in response to changes in the supply of N or C, and to changes in intracellular pH, using cultured Arabidopsis cells and seedlings. The results show that expression of both PPCK1 and PPCK2 is increased by C availability, but does not respond to N availability. Expression of the two PPCK genes and the phosphorylation state of PEPC are increased in response to increasing intracellular pH. Elevated pH also reduces the repression of PPCK gene expression by P-i. Expression of phosphoenolpyruvate carboxykinase (PEPCK), which catalyses the decarboxylation of oxaloacetate, is decreased in response to increasing intracellular pH. pH homeostasis may be mediated at least partly by reciprocal changes in the expression of PPCK genes and PEPCK.
引用
收藏
页码:1844 / 1850
页数:7
相关论文
共 40 条
[1]   Nitrogen acquisition, PEP carboxylase, and cellular pH homeostasis: new views on old paradigms [J].
Britto, DT ;
Kronzucker, HJ .
PLANT CELL AND ENVIRONMENT, 2005, 28 (11) :1396-1409
[2]   Disruption of the phosphate-starvation response of oilseed rape suspension cells by the fungicide phosphonate [J].
Carswell, MC ;
Grant, BR ;
Plaxton, WC .
PLANTA, 1997, 203 (01) :67-74
[3]   Phosphoenolpyruvate carboxykinase in cucumber plants is increased both by ammonium and by acidification, and is present in the phloem [J].
Chen, ZH ;
Walker, RP ;
Técsi, LI ;
Lea, PJ ;
Leegood, RC .
PLANTA, 2004, 219 (01) :48-58
[4]   BHLH32 modulates several biochemical and morphological processes that respond to Pi starvation in Arabidopsis [J].
Chen, Zhi-Hui ;
Nimmo, Gillian A. ;
Jenkins, Gareth I. ;
Nimmo, Hugh G. .
BIOCHEMICAL JOURNAL, 2007, 405 (01) :191-198
[5]   Phosphoenolpyruvate carboxylase: A ubiquitous, highly regulated enzyme in plants [J].
Chollet, R ;
Vidal, J ;
OLeary, MH .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1996, 47 :273-298
[6]   Phosphate status affects the gene expression, protein content and enzymatic activity of UDP-glucose pyrophosphorylase in wild-type and pho mutants of Arabidopsis [J].
Ciereszko, I ;
Johansson, H ;
Hurry, V ;
Kleczkowski, LA .
PLANTA, 2001, 212 (04) :598-605
[7]   THE FINE CONTROL OF CYTOSOLIC PH [J].
DAVIES, DD .
PHYSIOLOGIA PLANTARUM, 1986, 67 (04) :702-706
[8]   IN-VIVO REGULATION OF WHEAT-LEAF PHOSPHOENOLPYRUVATE CARBOXYLASE BY REVERSIBLE PHOSPHORYLATION [J].
DUFF, SMG ;
CHOLLET, R .
PLANT PHYSIOLOGY, 1995, 107 (03) :775-782
[9]   Arabidopsis thaliana contains two phosphoenolpyruvate carboxylase kinase genes with different expression patterns [J].
Fontaine, V ;
Hartwell, J ;
Jenkins, GI ;
Nimmo, HG .
PLANT CELL AND ENVIRONMENT, 2002, 25 (01) :115-122
[10]   Interaction between phosphate-starvation, sugar, and cytokinin signaling in arabidopsis and the roles of cytokinin receptors CRE1/AHK4 and AHK3 [J].
Franco-Zorrilla, JM ;
Martín, AC ;
Leyva, A ;
Par-Ares, JP .
PLANT PHYSIOLOGY, 2005, 138 (02) :847-857