Related Experiment Video
Updated: Jun 27, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
Involvement of the Pta-AckA pathway in protein folding and aggregation
Itzhak Mizrahi1, Dvora Biran, Eliora Z Ron
1Department of Molecular Microbiology & Biotechnology, The George S. Wise Faculty of Life Science, Tel Aviv University, Tel Aviv, Israel.
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 (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.
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
The Unfolded Protein Response

