Involvement of the Pta-AckA pathway in protein folding and aggregation.
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 (DeltaackApta) results in a very low cytoplasmic level of acetyl phosphate and impaired proteolysis. Here we show that the DeltaackApta 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.
Mizrahi
Itzhak
I
Department of Molecular Microbiology & Biotechnology, The George S. Wise Faculty of Life Science, Tel Aviv University, Tel Aviv, Israel.
Biran
Dvora
D
Ron
Eliora Z
EZ
D000255:Adenosine Triphosphate / Q000032:analysis; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D008156:Luciferases / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D009154:Mutation; D009876:Operon; D010755:Organophosphates / Q000378:metabolism*; D017510:Protein Folding
D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D010755:Organophosphates; C011632:acetyl phosphate; D000255:Adenosine Triphosphate; D008156:Luciferases