Modification of intracellular levels of glutathione-dependent formaldehyde dehydrogenase alters glutathione homeostasis and root development

被引:49
作者
Espunya, MC [1 ]
Díaz, M [1 ]
Moreno-Romero, J [1 ]
Martínez, MC [1 ]
机构
[1] Univ Autonoma Barcelona, Fac Ciencies, Dept Bioquim & Biol Mol, E-08193 Bellaterra, Barcelona, Spain
关键词
Arabidopis thaliana; immunolocalization; plants; S-nitrosoglutathione reductase;
D O I
10.1111/j.1365-3040.2006.01497.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Glutathione (GSH)-dependent formaldehyde dehydrogenase (FALDH) is a highly conserved medium-chain dehydrogenase reductase and the main enzyme that metabolizes intracellular formaldehyde in eukaryotes. It has been recently shown that it exhibits a strong S-nitrosoglutathione (GSNO) reductase activity and could be a candidate to regulate NO-signalling functions. However, there is a lack of knowledge about the tissue distribution of this enzyme in plants. Here, we have studied the localization and developmental expression of the enzyme using immunolocalization and histochemical activity assay methods. We conclude that FALDH is differentially expressed in the organs of Arabidopsis thaliana mature plants, with higher levels in roots and leaves from the first stages of development. Spatial distribution of FALDH in these two organs includes the main cell types [epidermis (Ep) and cortex (Cx) in roots, and mesophyll in leaves] and the vascular system. Arabidopsis thaliana mutants with modified levels of FALDH (both by over- and under-expression of the FALDH-encoding gene) show a significant reduction of root length, and this phenotype correlates with an overall decrease of intracellular GSH levels and alteration of spatial distribution of GSH in the root meristem. Transgenic roots are partially insensitive to exogenous GSH, suggesting an inability to detect reduction-oxidation (redox) changes of the GSH pool and/or maintain GSH homeostasis.
引用
收藏
页码:1002 / 1011
页数:10
相关论文
共 38 条
[1]   Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis [J].
Achkor, H ;
Díaz, M ;
Fernández, MR ;
Biosca, JA ;
Parés, X ;
Martínez, MC .
PLANT PHYSIOLOGY, 2003, 132 (04) :2248-2255
[2]   IMMUNOLOGICAL AND BIOCHEMICAL-CHARACTERIZATION OF THE HUMAN ALCOHOL-DEHYDROGENASE CHI-ADH ISOZYME [J].
ADINOLFI, A ;
ADINOLFI, M ;
HOPKINSON, DA .
ANNALS OF HUMAN GENETICS, 1984, 48 (JAN) :1-10
[3]   Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation [J].
Barber, RD ;
Donohue, TJ .
BIOCHEMISTRY, 1998, 37 (02) :530-537
[4]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[5]   STIMULATION BY PARAQUAT OF MICROSOMAL AND CYTOCHROME P-450-DEPENDENT OXIDATION OF GLYCEROL TO FORMALDEHYDE [J].
CLEJAN, LA ;
CEDERBAUM, AI .
BIOCHEMICAL JOURNAL, 1993, 295 :781-786
[6]   The glutathione-deficient, cadmium-sensitive mutant, cad2-1, of Arabidopsis thaliana is deficient in γ-glutamylcysteine synthetase. [J].
Cobbett, CS ;
May, MJ ;
Howden, R ;
Rolls, B .
PLANT JOURNAL, 1998, 16 (01) :73-78
[7]   Detoxification of xenobiotics in plant cells by glutathione conjugation and vacuolar compartmentalization: A fluorescent assay using monochlorobimane [J].
Coleman, JOD ;
Randall, R ;
BlakeKalff, MMA .
PLANT CELL AND ENVIRONMENT, 1997, 20 (04) :449-460
[8]   Histochemical assay to detect class III ADH activity in situ in Arabidopsis seedlings [J].
Díaz, M ;
Fernández, MR ;
Martínez, MC .
BIOTECHNIC & HISTOCHEMISTRY, 2004, 79 (02) :91-94
[9]   The gene encoding glutathione-dependent formaldehyde dehydrogenase/GSNO reductase is responsive to wounding, jasmonic acid and salicylic acid [J].
Díaz, M ;
Achkor, H ;
Titarenko, E ;
Martínez, MC .
FEBS LETTERS, 2003, 543 (1-3) :136-139
[10]  
Dolferus R, 1997, GENETICS, V146, P1131