Involvement of the Pta-AckA pathway in protein folding and aggregation

Itzhak Mizrahi; Dvora Biran; Eliora Z. Ron

doi:10.1016/j.resmic.2008.10.007

Involvement of the Pta-AckA pathway in protein folding and aggregation

Itzhak Mizrahi, Dvora Biran, Eliora Z. Ron

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

Acetyl phosphate is a central metabolite involved in a broad range of versatile cellular functions. Recently it was observed that in Escherichia coli the acetyl phosphate pathway is required for efficient ATP-dependent proteolysis. Deletion of the operon coding for acetyl phosphate metabolism (ΔackApta) results in a very low cytoplasmic level of acetyl phosphate and impaired proteolysis. Here we show that the ΔackApta mutation affects additional components of the protein quality control system. Thus, this deletion is accompanied by a decrease in protein refolding and rescue from aggregates. These results indicate the involvement of the acetyl phosphate pathway in chaperone capabilities, in addition to their effect on proteolysis.

Original language	English
Pages (from-to)	80-84
Number of pages	5
Journal	Research in Microbiology
Volume	160
Issue number	1
DOIs	https://doi.org/10.1016/j.resmic.2008.10.007
State	Published - 1 Jan 2009
Externally published	Yes

Keywords

Acetyl phosphate pathway
Chaperones
Heat shock response
Protein aggregation
Protein quality control

ASJC Scopus subject areas

Microbiology
Molecular Biology

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10.1016/j.resmic.2008.10.007

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title = "Involvement of the Pta-AckA pathway in protein folding and aggregation",

abstract = "Acetyl phosphate is a central metabolite involved in a broad range of versatile cellular functions. Recently it was observed that in Escherichia coli the acetyl phosphate pathway is required for efficient ATP-dependent proteolysis. Deletion of the operon coding for acetyl phosphate metabolism (ΔackApta) results in a very low cytoplasmic level of acetyl phosphate and impaired proteolysis. Here we show that the ΔackApta mutation affects additional components of the protein quality control system. Thus, this deletion is accompanied by a decrease in protein refolding and rescue from aggregates. These results indicate the involvement of the acetyl phosphate pathway in chaperone capabilities, in addition to their effect on proteolysis.",

keywords = "Acetyl phosphate pathway, Chaperones, Heat shock response, Protein aggregation, Protein quality control",

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

note = "Funding Information: We are grateful to Prof. Bernd Bukau for providing plasmid pBB516. This work was partially supported by the Manja and Morris Leigh Chair (EZR) for Biophysics and Biotechnology.",

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doi = "10.1016/j.resmic.2008.10.007",

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AU - Mizrahi, Itzhak

AU - Biran, Dvora

AU - Ron, Eliora Z.

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PY - 2009/1/1

Y1 - 2009/1/1

N2 - Acetyl phosphate is a central metabolite involved in a broad range of versatile cellular functions. Recently it was observed that in Escherichia coli the acetyl phosphate pathway is required for efficient ATP-dependent proteolysis. Deletion of the operon coding for acetyl phosphate metabolism (ΔackApta) results in a very low cytoplasmic level of acetyl phosphate and impaired proteolysis. Here we show that the ΔackApta mutation affects additional components of the protein quality control system. Thus, this deletion is accompanied by a decrease in protein refolding and rescue from aggregates. These results indicate the involvement of the acetyl phosphate pathway in chaperone capabilities, in addition to their effect on proteolysis.

AB - Acetyl phosphate is a central metabolite involved in a broad range of versatile cellular functions. Recently it was observed that in Escherichia coli the acetyl phosphate pathway is required for efficient ATP-dependent proteolysis. Deletion of the operon coding for acetyl phosphate metabolism (ΔackApta) results in a very low cytoplasmic level of acetyl phosphate and impaired proteolysis. Here we show that the ΔackApta mutation affects additional components of the protein quality control system. Thus, this deletion is accompanied by a decrease in protein refolding and rescue from aggregates. These results indicate the involvement of the acetyl phosphate pathway in chaperone capabilities, in addition to their effect on proteolysis.

KW - Acetyl phosphate pathway

KW - Chaperones

KW - Heat shock response

KW - Protein aggregation

KW - Protein quality control

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DO - 10.1016/j.resmic.2008.10.007

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JO - Research in Microbiology

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Involvement of the Pta-AckA pathway in protein folding and aggregation

Abstract

Keywords

ASJC Scopus subject areas

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