Physical characterization of the cloned protease III gene from Escherichia coli K-12.

Abstract

Analysis of the cloned protease III gene (ptr) from Escherichia coli K-12 has demonstrated that in addition to the previously characterized 110,000-Mr protease III protein, a second 50,000-Mr polypeptide (p50) is derived from the amino-terminal end of the coding sequence. The p50 polypeptide is found predominantly in the periplasmic space along with protease III, but does not proteolytically degrade insulin, a substrate for protease III. p50 does not appear to originate from autolysis of the larger protein. Protease III is not essential for normal cell growth since deletion of the structural gene causes no observed alterations in the phenotypic properties of the bacteria. A 30-fold overproduction of protease III does not affect cell viability. A simple new purification method for protease III is described.

• Authors: C C Dykstra, S R Kushner
• Journal: Journal of bacteriology (J Bacteriol) Vol. 163 Issue 3 Pg. 1055-9 (Sep 1985) ISSN: 0021-9193 [Print] United States
• PMID: 2993229 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Sulfur Radioisotopes
• Methionine
• DNA Restriction Enzymes
• Endopeptidases
• Metalloendopeptidases
• pitrilysin

Topics

• Cloning, Molecular
• DNA Restriction Enzymes
• Endopeptidases (biosynthesis, genetics)
• Escherichia coli (enzymology, genetics)
• Genes
• Genes, Bacterial
• Kinetics
• Metalloendopeptidases
• Methionine (metabolism)
• Plasmids
• Sulfur Radioisotopes