@article{cac614b287aa458881f96bbc75cdbda8,
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.",
year = "2009",
month = jan,
doi = "10.1016/j.resmic.2008.10.007",
language = "אנגלית",
volume = "160",
pages = "80--84",
journal = "Research in Microbiology",
issn = "0923-2508",
publisher = "Elsevier Masson s.r.l.",
number = "1",
}