SPP 1132:  Proteolysis in Prokaryotes: Protein Quality Control and Regulatory Principle

Recent research has demonstrated that the controlled destruction of specific proteins, i.e. proteolysis, plays a key role in global cellular regulation in all types of living cells. The priority program aims at understanding the molecular structures and mechanisms as well as the regulation and physiological functions of protein degradation in bacteria and organells of prokaryotic origin (such as mitochondria and chloroplasts). Controlled proteolysis as a novel regulatory principle is being investigated in the context of stress responses, differentiation, cell cycle and virulence of pathogenic bacteria. In addition, proteolysis provides an exquisitely regulated protein quality control mechanism that eliminates denatured, aggregated or incomplete polypeptides. It is of special interest to identify novel proteins that are regulated by proteolysis and to study protein recognition by chaperone/protease systems in molecular detail. Moreover, the program will focus on signal transduction and regulatory mechanisms that control degradation of specific proteins (such as key regulators of gene expression networks) in response to extra- and intracellular signals. The experimental approaches chosen are interdisciplinary and incluce microbiology, genetics, molecular biology, biochemistry, structural biology as well as genomics and proteomics.

DFG Programme Priority Programmes

• Analysis of the role of HSP100/Clp and their adaptor proteins in general and regulated proteolysis in Bacillus subtilis (Applicant Turgay, Kürsad )
• Characterization of the archaeal membrane-associated Lon protease (Applicant Zwickl, Peter )
• Function of the ATP-dependent metalloprotease FtsH during sporulation of Bacillus subtilis (Applicant Schumann, Wolfgang )
• Functional characterization of mitochondrial AAA proteases in Saccharomyces cerevisiae (Applicant Langer, Thomas )
• Global characterization of the substrate spectrum of the Corynebacterium glutamicum Clp protease (Applicant Schaffer, Steffen )
• Global regulation by proteolysis in Escherichia coli: Molecular recognition, signal integration and quantitative analysis of proteolysis-controlled regulatory circuits (Applicant Hengge, Regine )
• Mechanisms of protease-substrate interactions in the E. coli cytosol (Applicant Bukau, Bernd )
• Nitrogen-starvation induced chlorosis in cyanobacteria: A proteolytic program for maintenance of viability (Applicant Forchhammer, Karl )
• Role of prohibitins for proteolytic processes within mitochondria (Applicant Langer, Thomas )
• structural sudies of ClpS, dem RpoS/RssB-Target System und FtsH (Applicant Zeth, Kornelius )
• Structure and function of HxH metalloproteases (Applicant Bochtler, Matthias )
• Structure-function analysis of DegP and DegS (Applicant Ehrmann, Michael )
• Structure-Function Analysis of the Heat Shock Protein DegP (Applicant Clausen, Tim )
• Substrate selection by the FtsH protease (Applicant Narberhaus, Franz )
• The functionals role of AAA+ proteases as central components of the mitochondrial protein quality control network under normal and stress conditions (Applicant Voos, Wolfgang )

Spokesperson Professorin Dr. Regine Hengge