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Escherichia coli HdeB is an acid stress chaperone.
We cloned, expressed, and purified the hdeB gene product, which belongs to the hdeAB acid stress operon. We extracted HdeB from bacteria by the osmotic-shock procedure and purified it to homogeneityExpand
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Peptidase Activity of the Escherichia coli Hsp31 Chaperone*
Hsp31, the Escherichia coli hcha gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperature. Its crystal structure reveals a putative Cys184, His185, and Asp213Expand
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YhbO protects cells against multiple stresses.
YhbO is a member of the DJ-1/ThiJ/Pfp1 superfamily, which includes chaperones, peptidases, and the Parkinson's disease protein DJ-1. A yhbO-disrupted mutant of Escherichia coli is highly sensitive toExpand
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Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB*
The acid stress chaperones HdeA and HdeB of Escherichia coli prevent the aggregation of periplasmic proteins at acidic pH. We show in this report that they also form mixed aggregates with proteinsExpand
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  • Open Access
Characterization of the Escherichia coli YedU protein as a molecular chaperone.
We have cloned, purified to homogeneity, and characterized as a molecular chaperone the Escherichia coli YedU protein. The purified protein shows a single band at 31 kDa on SDS-polyacrylamide gelsExpand
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Guanine glycation repair by DJ-1/Park7 and its bacterial homologs
Not-so-sweet DNA damage repaired Glyoxal and methylglyoxal, by-products of sugar metabolism that are present in all cells, can react with, and thus damage, DNA. Indeed, glycation of guanine (G) is asExpand
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  • Open Access
The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal.
Hsp31 belongs to the PfpI/Hsp31/DJ-1 superfamily, and has been reported to display chaperone, peptidase and glutathione-independent glyoxalase activities. Here, we show that Hsp31 repairs glyoxal-Expand
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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- andExpand
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Cloning, expression, and purification of the general stress protein YhbO from Escherichia coli.
We cloned, expressed, and purified the Escherichia coli yhbO gene product, which is an amino acid sequence homolog to the Bacillus subtilis general stress protein 18 (the yfkM gene product), theExpand
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  • Open Access
The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase.
Escherichia coli contains two thioredoxins, Trx1 and Trx2, and a thioredoxin-like protein, YbbN, which presents a strong homology in its N-terminal part with thioredoxins, and possesses a 20kDaExpand
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