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

Itzhak Mizrahi, Dvora Biran, Eyal Gur, Eliora Z. Ron

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)82-85
Number of pages4
JournalJournal of Microbiological Methods
Volume70
Issue number1
DOIs
StatePublished - Jul 2007

Keywords

  • Escherichia coli
  • Heat shock response
  • Homoserine trans-succinylase
  • Protein quality control
  • Proteolysis

Fingerprint

Dive into the research topics of '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'. Together they form a unique fingerprint.

Cite this