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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 31, Number 6
BKCSDE 31(6)
June 20, 2010 

 
Title
Mutational Analysis of the Metal-binding Sites of Peroxide Sensor PerR
Author
Young Bin Won, Chang Jun Ji, Ju Hyun Cho*, Jin Won Lee*
Keywords
PerR, Bacillus subtilis, Peroxide, Metal, Transcription factor
Abstract
Bacillus subtilis PerR is a metal-dependent peroxide-sensing transcription factor which uses metal-catalyzed histidine oxidation for peroxide-sensing. PerR contains two metal binding sites, one for structural Zn2+ and the other for the regulatory/ peroxide-sensing metal. Here we investigated the effect of mutations at both the structural and regulatory metal binding sites on the oxidation of either H37 or H91, two of the peroxide-sensing ligands. All four serine substitution mutants at the structural Zn2+ site (C96S, C99S, C136S and C139S) exhibited no detectable oxidation at histidine residues. Two of the alanine substitution mutants at regulatory metal site (H37A and D85A) exhibited selective oxidation preferentially at the H91-containing tryptic peptide, whereas no oxidation was detected in the other mutants (H91A, H93A and D104A). Our results suggest that the cysteine residues coordinating structural Zn2+ are essential for peroxide sensing by PerR, and that the C-terminal regulatory metal binding site composed of H91, H93 and D104 can bind Fe2+, providing a possible explanation for the peroxide sensing mechanisms by PerR.
Page
1573 - 1576
Full Text
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