The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal

被引：34
作者：
Abdallah, Jad [1 ,2 ]
Mihoub, Mouadh [1 ]
Gautier, Valerie [1 ]
Richarme, Gilbert [1 ]
机构：
[1] Univ Paris 07, CNRS UMR 7592, Inst Jacques Monod, Stress Mol, 15 Rue Helene Brion, F-75013 Paris, France
[2] Lebanese Amer Univ, Sch Pharm, Byblos, Lebanon
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2016年 / 470卷 / 02期
关键词：
Electrophile stress; Carbonyl stress; Glycation; Maillard reaction; Protein repair; MOLECULAR CHAPERONE; PROKARYOTIC HOMOLOG; PROTECTS CELLS; HSP31; STRESS;
D O I：
10.1016/j.bbrc.2016.01.068
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：
YhbO and YajL belong to the PfpI/Hsp31/DJ-1 superfamily. Both proteins are involved in protection against environmental stresses. Here, we show that, like DJ-1 and Hsp31, they repair glyoxal- and methylglyoxal-glycated proteins. YhbO and YajL repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. Moreover, yhbO and yajL mutants display decreased viability in methylglyoxal- or glucose containing media. Finally, the apparent glyoxalase activities of YhbO and YajL reflect their deglycase activities. (C) 2016 Elsevier Inc. All rights reserved.
引用
收藏
页码：282 / 286
页数：5
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