Details
| Original language | English |
|---|---|
| Pages (from-to) | 1323-1327 |
| Number of pages | 5 |
| Journal | SCIENCE |
| Volume | 324 |
| Issue number | 5932 |
| Publication status | Published - 2009 |
| Externally published | Yes |
Abstract
All living organisms face a variety of environmental stresses thafdause the misfolding and aggregation of proteins. To eliminate damaged proteins, cells developed highly efficient stress response and protein quality control systems. We performed a biochemical and structural analysis of the bacterial CtsR/AAcsB stress response. The crystal structure of the CtsR repressor, in complex with DNA, pinpointed key residues important for high-affinity binding to the promoter regions of heat-shock genes. Moreover, biochemical characterization of McsB revealed that McsB specifically phosphorylates arginine residues in the DNA binding domain of CtsR, thereby impairing its function as a repressor of stress response genes. Identification of the CtsR/AAcsB arginine phospho-switch expands the repertoire of possible protein modifications involved in prokaryotic and eukaryotic transcriptional regulation.
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In: SCIENCE, Vol. 324, No. 5932, 2009, p. 1323-1327.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - McsB Is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator ctsr
AU - Fuhrmann, Jakob
AU - Schmidt, Andreas
AU - Spiess, Silvia
AU - Lehner, Anita
AU - Turgay, Kursad
AU - Mechtler, Karl
AU - Charpentier, Emmanuelle
AU - Clausen, Tim
N1 - Copyright: Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2009
Y1 - 2009
N2 - All living organisms face a variety of environmental stresses thafdause the misfolding and aggregation of proteins. To eliminate damaged proteins, cells developed highly efficient stress response and protein quality control systems. We performed a biochemical and structural analysis of the bacterial CtsR/AAcsB stress response. The crystal structure of the CtsR repressor, in complex with DNA, pinpointed key residues important for high-affinity binding to the promoter regions of heat-shock genes. Moreover, biochemical characterization of McsB revealed that McsB specifically phosphorylates arginine residues in the DNA binding domain of CtsR, thereby impairing its function as a repressor of stress response genes. Identification of the CtsR/AAcsB arginine phospho-switch expands the repertoire of possible protein modifications involved in prokaryotic and eukaryotic transcriptional regulation.
AB - All living organisms face a variety of environmental stresses thafdause the misfolding and aggregation of proteins. To eliminate damaged proteins, cells developed highly efficient stress response and protein quality control systems. We performed a biochemical and structural analysis of the bacterial CtsR/AAcsB stress response. The crystal structure of the CtsR repressor, in complex with DNA, pinpointed key residues important for high-affinity binding to the promoter regions of heat-shock genes. Moreover, biochemical characterization of McsB revealed that McsB specifically phosphorylates arginine residues in the DNA binding domain of CtsR, thereby impairing its function as a repressor of stress response genes. Identification of the CtsR/AAcsB arginine phospho-switch expands the repertoire of possible protein modifications involved in prokaryotic and eukaryotic transcriptional regulation.
UR - http://www.scopus.com/inward/record.url?scp=66749180668&partnerID=8YFLogxK
U2 - 10.1126/science.1170088
DO - 10.1126/science.1170088
M3 - Article
C2 - 19498169
AN - SCOPUS:66749180668
VL - 324
SP - 1323
EP - 1327
JO - SCIENCE
JF - SCIENCE
SN - 0036-8075
IS - 5932
ER -