McsB Is a Protein Arginine Kinase That Phosphorylates and Inhibits the Heat-Shock Regulator CtsR
2009; American Association for the Advancement of Science; Volume: 324; Issue: 5932 Linguagem: Inglês
10.1126/science.1170088
ISSN1095-9203
AutoresJakob Fuhrmann, Andreas Schmidt, Silvia Spiess, Anita Lehner, Kürşad Turgay, Karl Mechtler, Emmanuelle Charpentier, Tim Clausen,
Tópico(s)Protein Structure and Dynamics
ResumoAll living organisms face a variety of environmental stresses that cause 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/McsB 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/McsB arginine phospho-switch expands the repertoire of possible protein modifications involved in prokaryotic and eukaryotic transcriptional regulation.
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