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PMID: 323853 Published · ppublish English Journal Article

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

Inouye H, Beckwith J

Abstract

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.

MeSH Terms
Alkaline Phosphatase/biosynthesis Cell Membrane/enzymology Enzyme Precursors/biosynthesis Escherichia coli/enzymology Galactosidases/biosynthesis Genes Protein Biosynthesis
Chemicals
Enzyme Precursors Alkaline Phosphatase Galactosidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Inouye H
Beckwith J
References (24)
24 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1977-04-00
Pages
1440-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430790
Subset
IM
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