Control of protein function through regulated protein degradation: biotechnological and biomedical applications.
Targeted protein degradation is crucial for the correct function and maintenance of a cell. In bacteria, this process is largely performed by a handful of ATP-dependent machines, which generally consist of two components - an unfoldase and a peptidase. In some cases, however, substrate recognition by the protease may be regulated by specialized delivery factors (known as adaptor proteins). Our detailed understanding of how these machines are regulated to prevent uncontrolled degradation within a cell has permitted the identification of novel antimicrobials that dysregulate these machines, as well as the development of tunable degradation systems that have applications in biotechnology. Here, we focus on the physiological role of the ClpP peptidase in bacteria, its role as a novel antibiotic target and the use of protein degradation as a biotechnological approach to artificially control the expression levels of a protein of interest.
Department of Biochemistry, La Trobe Institute for Molecular Science LIMS, La Trobe University, Melbourne, Vic., Australia.
Jyotsna
J
Nagpal
Ju Lin
JL
Tan
Kaye N
KN
Truscott
Begoña
B
Heras
David A
DA
Dougan
D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D020811:Biomedical Technology / Q000379:methods; D001709:Biotechnology / Q000379:methods; D049071:Endopeptidase Clp / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D059748:Proteolysis
D001426:Bacterial Proteins; D049071:Endopeptidase Clp