TY - JOUR
T1 - Tools for the study of protein quality control systems
T2 - Use of truncated homoserine trans-succinylase as a model substrate for ATP-dependent proteolysis in Escherichia coli
AU - Mizrahi, Itzhak
AU - Biran, Dvora
AU - Gur, Eyal
AU - Ron, Eliora Z.
N1 - Funding Information:
This work was partially supported by the Manja and Morris Leigh Chair for Biophysics and Biotechnology.
PY - 2007/7/1
Y1 - 2007/7/1
N2 - 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 HTSΔ1-6, 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.
AB - 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 HTSΔ1-6, 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.
KW - Escherichia coli
KW - Heat shock response
KW - Homoserine trans-succinylase
KW - Protein quality control
KW - Proteolysis
UR - http://www.scopus.com/inward/record.url?scp=34250715805&partnerID=8YFLogxK
U2 - 10.1016/j.mimet.2007.03.012
DO - 10.1016/j.mimet.2007.03.012
M3 - Article
AN - SCOPUS:34250715805
SN - 0167-7012
VL - 70
SP - 82
EP - 85
JO - Journal of Microbiological Methods
JF - Journal of Microbiological Methods
IS - 1
ER -