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

doi:10.1016/j.mimet.2007.03.012

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 journal › Article › peer-review

1 Scopus citations

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 HTS_Δ1-6, 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 language	English
Pages (from-to)	82-85
Number of pages	4
Journal	Journal of Microbiological Methods
Volume	70
Issue number	1
DOIs	https://doi.org/10.1016/j.mimet.2007.03.012
State	Published - 1 Jul 2007
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Microbiology
Molecular Biology
Microbiology (medical)

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10.1016/j.mimet.2007.03.012

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title = "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",

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.",

keywords = "Escherichia coli, Heat shock response, Homoserine trans-succinylase, Protein quality control, Proteolysis",

author = "Itzhak Mizrahi and Dvora Biran and Eyal Gur and Ron, {Eliora Z.}",

note = "Funding Information: This work was partially supported by the Manja and Morris Leigh Chair for Biophysics and Biotechnology.",

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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

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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

Abstract

Keywords

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