Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 53 - 59 |
| Number of pages | 7 |
| Journal | Nature Chemical Biology |
| Volume | 5 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2009 |
| Externally published | Yes |
Cite this
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Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein. / Traore, Daouda A K; El Ghazouani, Abdelnasser; Jacquamet, Lilian; Borel, Franck; Ferrer, Jean -Luc; Lascoux, David; Ravanat, Jean -Luc; Jaquinod, Michel; Blondin, Genevieve; Caux-Thang, Christelle; Duarte, Victor; Latour, Jean -Marc.
In: Nature Chemical Biology, Vol. 5, No. 1, 2009, p. 53 - 59.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein
AU - Traore, Daouda A K
AU - El Ghazouani, Abdelnasser
AU - Jacquamet, Lilian
AU - Borel, Franck
AU - Ferrer, Jean -Luc
AU - Lascoux, David
AU - Ravanat, Jean -Luc
AU - Jaquinod, Michel
AU - Blondin, Genevieve
AU - Caux-Thang, Christelle
AU - Duarte, Victor
AU - Latour, Jean -Marc
PY - 2009
Y1 - 2009
N2 - In Bacillus subtilis, PerR is a metal-dependent sensor of hydrogen peroxide. PerR is a dimeric zinc protein with a regulatory site that coordinates either Fe2+ (PerR-Zn-Fe) or Mn2+ (PerR-Zn-Mn). Though most of the peroxide sensors use cysteines to detect H2O2, it has been shown that reaction of PerR-Zn-Fe with H2O2 leads to the oxidation of one histidine residue. Oxidation of PerR leads to the incorporation of one oxygen atom into His37 or His91. This study presents the crystal structure of the oxidized PerR protein (PerR-Zn-ox), which clearly shows a 2-oxo-histidine residue in position 37. Formation of 2-oxo-histidine is demonstrated and quantified by HPLC-MS/MS. EPR experiments indicate that PerR-Zn-H37ox retains a significant affinity for the regulatory metal, whereas PerR-Zn-H91ox shows a considerably reduced affinity for the metal ion. In spite of these major differences in terms of metal binding affinity, oxidation of His37 and/or His91 in PerR prevents DNA binding.
AB - In Bacillus subtilis, PerR is a metal-dependent sensor of hydrogen peroxide. PerR is a dimeric zinc protein with a regulatory site that coordinates either Fe2+ (PerR-Zn-Fe) or Mn2+ (PerR-Zn-Mn). Though most of the peroxide sensors use cysteines to detect H2O2, it has been shown that reaction of PerR-Zn-Fe with H2O2 leads to the oxidation of one histidine residue. Oxidation of PerR leads to the incorporation of one oxygen atom into His37 or His91. This study presents the crystal structure of the oxidized PerR protein (PerR-Zn-ox), which clearly shows a 2-oxo-histidine residue in position 37. Formation of 2-oxo-histidine is demonstrated and quantified by HPLC-MS/MS. EPR experiments indicate that PerR-Zn-H37ox retains a significant affinity for the regulatory metal, whereas PerR-Zn-H91ox shows a considerably reduced affinity for the metal ion. In spite of these major differences in terms of metal binding affinity, oxidation of His37 and/or His91 in PerR prevents DNA binding.
UR - http://www.nature.com/nchembio/journal/v5/n1/pdf/nchembio.133.pdf
U2 - 10.1038/nchembio.133
DO - 10.1038/nchembio.133
M3 - Article
VL - 5
SP - 53
EP - 59
JO - Nature Chemical Biology
JF - Nature Chemical Biology
SN - 1552-4450
IS - 1
ER -