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
[31]   SIMPLE DETERMINATION OF FORMALDEHYDE IN DIMEDONE ADDUCT FORM IN BIOLOGICAL SAMPLES BY HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY [J].
SARDI, E ;
TYIHAK, E .
BIOMEDICAL CHROMATOGRAPHY, 1994, 8 (06) :313-314
[32]   Pea formaldehyde-active class III alcohol dehydrogenase: Common derivation of the plant and animal forms but not of the corresponding ethanol-active forms (classes I and P) [J].
Shafqat, J ;
ElAhmad, M ;
Danielsson, O ;
Martinez, MC ;
Persson, B ;
Pares, X ;
Jornvall, H .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (11) :5595-5599
[33]   REDOX SIGNALING - NITROSYLATION AND RELATED TARGET INTERACTIONS OF NITRIC-OXIDE [J].
STAMLER, JS .
CELL, 1994, 78 (06) :931-936
[34]   PURIFICATION OF FORMALDEHYDE AND FORMATE DEHYDROGENASES FROM PEA-SEEDS BY AFFINITY CHROMATOGRAPHY AND S-FORMYLGLUTATHIONE AS THE INTERMEDIATE OF FORMALDEHYDE METABOLISM [J].
UOTILA, L ;
KOIVUSALO, M .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1979, 196 (01) :33-45
[35]  
Uotila L, 1989, COENZYMES COFACTOR A, V3, P517
[36]   The ROOT MERISTEMLESS1/CADMIUM SENSITIVE2 gene defines a glutathione-dependent pathway involved in initiation and maintenance of cell division during postembryonic root development [J].
Vernoux, T ;
Wilson, RC ;
Seeley, KA ;
Reichheld, JP ;
Muroy, S ;
Brown, S ;
Maughan, SC ;
Cobbett, CS ;
Van Montagu, M ;
Inzé, D ;
May, MJ ;
Sung, ZR .
PLANT CELL, 2000, 12 (01) :97-109
[37]   Maize glutathione-dependent formaldehyde dehydrogenase: protein sequence and catalytic properties [J].
Wippermann, U ;
Fliegmann, J ;
Bauw, G ;
Langebartels, C ;
Maier, K ;
Sandermann, H .
PLANTA, 1999, 208 (01) :12-18
[38]   The biological functions of glutathione revisited in Arabidopsis transgenic plants with altered glutathione levels [J].
Xiang, CB ;
Werner, BL ;
Christensen, EM ;
Oliver, DJ .
PLANT PHYSIOLOGY, 2001, 126 (02) :564-574