title: Proteomic methods unravel the protein quality control in Escherichia coli.
abstract: Protein quality control is an essential process in all living organisms. A network of folding helper proteins and proteases ushers proteins into their native conformation, safeguards their structure under adverse environmental conditions, and, if all else fails, degrades proteins at the end of their life time. Escherichia coli is a versatile model organism used in the analysis of fundamental cellular processes. Much of what we know about protein quality control has been discovered in this microorganism. In the investigation of the mode of action, regulation and substrate specificity of chaperones, thiol-disulfide isomerases and proteases, proteomic methods have been playing a key role. Here, we provide a condensed overview about the protein quality control network in E. coli and the remarkable contributions of proteomics to our current knowledge.
authors.affiliation: Ruhr-Universität Bochum, Medizinisches Proteom-Center, Redox-Proteomics Group, Bochum, Germany. lars.leichert@ruhr-uni-bochum.de
authors.forename: Lars I
authors.initials: LI
authors.lastname: Leichert
mesh_terms: D029968:Escherichia coli Proteins / Q000378:metabolism*; D008954:Models, Biological; D018832:Molecular Chaperones; D040901:Proteomics / Q000379:methods*
chemical_list: D029968:Escherichia coli Proteins; D018832:Molecular Chaperones