Novel alkenal/one reductase activity of yeast NADPH:quinone reductase Zta1p. Prospect of the functional role for the ζ-crystallin family

被引:12
作者
Crosas, Eva [1 ]
Porte, Sergio [1 ]
Moeini, Agrin [1 ]
Farres, Jaume [1 ]
Biosca, Josep. A. [1 ]
Pares, Xavier [1 ]
Rosario Fernandez, M. [1 ]
机构
[1] Univ Autonoma Barcelona, Fac Biosci, Dept Biochem & Mol Biol, E-08193 Barcelona, Spain
关键词
Alkenal/one reductase; Quinone oxidoreductase; Double-bond alpha; beta-hydrogenation; Medium-chain dehydrogenases/reductases; zeta-Crystallin; ZTA1; OXIDOREDUCTASE; NADPH; IDENTIFICATION; INACTIVATION; PURIFICATION; INCREASE; PROTEIN; LENS;
D O I
10.1016/j.cbi.2011.01.021
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
zeta-Crystallins are a Zn2+-lacking enzyme group with quinone reductase activity, which belongs to the medium-chain dehydrogenase/reductase superfamily. It has been recently observed that human zeta-crystallin is capable of reducing the alpha,beta-double bond of alkenals and alkenones. Here we report that this activity is also shared by the homologous Zta1p enzyme from Saccharomyces cerevisiae. While the two enzymes show similar substrate specificity, human zeta-crystallin exhibits higher activity with lipid peroxidation products and Zta1p is more active with cinnamaldehyde. The presence of Zta1p has an in vivo protective effect on yeast strains exposed to the toxic substrate 3-penten-2-one. Analysis of ZTA1 gene expression indicates an induction under different types of cellular stress, including ethanol and dimethylsulfoxide exposure and by reaching the stationary growth phase. The role of Zta1p in the yeast adaptation to some stress types and the general functional significance of zeta-crystallins are discussed. (C) 2011 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码:32 / 37
页数:6
相关论文
共 27 条
[1]   Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: New insights into its substrate recognition properties [J].
Chen, Zhi-Jun ;
Pudas, Regina ;
Sharma, Satyan ;
Smart, Oliver S. ;
Juffer, Andre H. ;
Hiltunen, J. Kalervo ;
Wierenga, Rik K. ;
Haapalainen, Antti M. .
JOURNAL OF MOLECULAR BIOLOGY, 2008, 379 (04) :830-844
[2]   Oxidoreductases in lipoxin A4 metabolic inactivation -: A novel role for 15-oxoprostaglandin 13-reductase/leukotriene B4 12-hydroxydehydrogenase in inflammation [J].
Clish, CB ;
Levy, BD ;
Chiang, N ;
Tai, HH ;
Serhan, CN .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (33) :25372-25380
[3]   Antioxidative function and substrate specificity of NAD(P)H-dependent alkenal/one oxidoreductase -: A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase [J].
Dick, RA ;
Kwak, MK ;
Sutter, TR ;
Kensler, TW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (44) :40803-40810
[4]   Tolerance and stress response to ethanol in the yeast Saccharomyces cerevisiae [J].
Ding, Junmei ;
Huang, Xiaowei ;
Zhang, Lemin ;
Zhao, Na ;
Yang, Dongmei ;
Zhang, Keqin .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2009, 85 (02) :253-263
[5]   Purification, cDNA cloning and expression of 15-oxoprostaglandin 13-reductase from pig lung [J].
Ensor, CM ;
Zhang, HX ;
Tai, HH .
BIOCHEMICAL JOURNAL, 1998, 330 :103-108
[6]   Human and yeast ζ-crystallins bind AU-rich elements in RNA [J].
Fernandez, M. R. ;
Porte, S. ;
Crosas, E. ;
Barbera, N. ;
Farres, J. ;
Biosca, J. A. ;
Pares, X. .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2007, 64 (11) :1419-1427
[7]  
HIEFSKI T, 2003, HOLZFORSCHUNG, V57, P479
[8]   ZETA-CRYSTALLIN, A NOVEL LENS PROTEIN FROM THE GUINEA-PIG [J].
HUANG, QL ;
RUSSELL, P ;
STONE, SH ;
ZIGLER, JS .
CURRENT EYE RESEARCH, 1987, 6 (05) :725-732
[9]   ZETA-CRYSTALLIN VERSUS OTHER MEMBERS OF THE ALCOHOL-DEHYDROGENASE SUPER-FAMILY - VARIABILITY AS A FUNCTIONAL CHARACTERISTIC [J].
JORNVALL, H ;
PERSSON, B ;
DUBOIS, GC ;
LAVERS, GC ;
CHEN, JH ;
GONZALEZ, P ;
RAO, PV ;
ZIGLER, JS .
FEBS LETTERS, 1993, 322 (03) :240-244
[10]   INITIAL REACTIONS IN THE FUNGAL DEGRADATION OF GUAIACYLGLYCEROL-BETA-CONIFERYL ETHER, A LIGNIN SUBSTRUCTURE MODEL [J].
KATAYAMA, T ;
NAKATSUBO, F ;
HIGUCHI, T .
ARCHIVES OF MICROBIOLOGY, 1980, 126 (02) :127-132