The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal
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...
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Veröffentlicht in: | Biochemical and biophysical research communications 2016-02, Vol.470 (2), p.282-286 |
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Sprache: | eng |
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Zusammenfassung: | 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.
•Hsp31, YhbO and YajL in Escherichia coli repair proteins form glycation.•This is a repair from glycation by the dicarbonyls glyoxal and methylglyoxal.•Triple mutant displays 10-fold increased glycation levels and 100-fold viability loss. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/j.bbrc.2016.01.068 |