Tools for the study of protein quality control systems: use of truncated homoserine trans-succinylase as a model substrate for ATP-dependent proteolysis in Escherichia coli.
Protein quality control, mediated by chaperones and ATP-dependent proteases, is essential for maintaining balanced growth and for regulating critical processes. To study these systems it is necessary to have model substrate proteins. However, most cellular proteins are stable and the few unstable proteins are usually regulatory and present in low concentrations, making them unsuitable for studies, especially in vivo. We present HTS(Delta1-6), a truncated homoserine trans-succinylase (HTS) which is unstable, can be expressed at high levels and has an enzymatic, measurable, activity. This protein can serve as a good model substrate for Escherichia coli ATP-dependent proteolysis.
Mizrahi
Itzhak
I
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv, 69978 Israel.
Biran
Dvora
D
Gur
Eyal
E
Ron
Eliora Z
EZ
D049069:ATP-Dependent Proteases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D018869:Heat-Shock Response; D051082:Homoserine O-Succinyltransferase / Q000235:genetics / Q000378:metabolism*; D008967:Molecular Biology / Q000379:methods*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D051082:Homoserine O-Succinyltransferase; C494973:metA protein, E coli; D049069:ATP-Dependent Proteases