Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro.

作者：Hiroshi Inouye, Jon Beckwith · 发表于：Proceedings of the National Academy of Sciences · 年份：1977 · DOI：10.1073/pnas.74.4.1440 · 被引用次数：170 · 研究领域：Pancreatic function and diabetes、Endoplasmic Reticulum Stress and Disease、Growth Hormone and Insulin-like Growth Factors

Alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] of E. coli was synthesized in a cell-free system, and the size of the direct translation product was analyzed. The product has a higher molecular weight than the mature alkaline phosphatase found in the periplasm. The direct translation product can be processed to the mature size by an E. coli membrane fraction; the processing activity copurifies with the outer-membrane fraction. The presumed precursor can dimerize to form active enzyme without being processed, and the resultant enzyme appears to be more hydrophobic than the mature enzyme. These findings are discussed in connection with the "signal hypothesis" proposed for the excretion of proteins across membranes.