Extracellular Release of Colicin A is Non-specific

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 1987 Aug 1

PMID 3311727

Citations 19

Authors

D Baty

R Lloubes

V Geli

C Lazdunski

S P Howard

Affiliations

Soon will be listed here.

Abstract

The possible involvement of topogenic export sequences within the colicin A polypeptide chain has been investigated. Different constructs have been made using various techniques to introduce deletions in the central and NH2-terminal regions of colicin A. Together, these deletions span the region from amino acid 15 to the end of the protein. None of these regions was found to be required for extracellular release or had any effect on the efficiency of this process. By inserting a termination codon, a Shine-Dalgarno sequence and an initiation codon into the gene for colicin A, the NH2-terminal and central plus COOH-terminal domains could be demonstrated to be released to the same extent when produced as separate polypeptides as when produced as linked ones. The introduction into the COOH-terminal domain of mutations promoting cytoplasmic aggregation had no effect on the secretion of the NH2-terminal polypeptide. These results demonstrated that no specific interaction between the NH2- and COOH-terminal regions of the colicin A polypeptide chain is involved in the release of colicin A. We are led to conclude that there is no topogenic export signal in the polypeptide chain of colicin A involved in the release mechanism. Thus the process is non-specific with respect to the colicin itself and depends solely on the expression of the colicin A lysis protein (Cavard et al., 1985, 1987). The expression of the protein causes the release of not only the colicin but also many other cellular proteins, including beta-lactamase, EF-Tu, and chloramphenicol acetyltransferase.

Citing Articles

Colicin biology.

Cascales E, Buchanan S, Duche D, Kleanthous C, Lloubes R, Postle K Microbiol Mol Biol Rev. 2007; 71(1):158-229.

PMID: 17347522 PMC: 1847374. DOI: 10.1128/MMBR.00036-06.

Assembly of colicin A in the outer membrane of producing Escherichia coli cells requires both phospholipase A and one porin, but phospholipase A is sufficient for secretion.

Cavard D J Bacteriol. 2002; 184(13):3723-33.

PMID: 12057969 PMC: 135121. DOI: 10.1128/JB.184.13.3723-3733.2002.

Genetic organization of plasmid ColJs, encoding colicin Js activity, immunity, and release genes.

Smajs D, Weinstock G J Bacteriol. 2001; 183(13):3949-57.

PMID: 11395458 PMC: 95277. DOI: 10.1128/JB.183.13.3949-3957.2001.

Colicins--exocellular lethal proteins of Escherichia coli.

Smarda J, Smajs D Folia Microbiol (Praha). 1999; 43(6):563-82.

PMID: 10069005 DOI: 10.1007/BF02816372.

In vivo analysis of sequence requirements for processing and degradation of the colicin A lysis protein signal peptide.

Howard S, Lindsay L J Bacteriol. 1998; 180(12):3026-30.

PMID: 9620949 PMC: 107800. DOI: 10.1128/JB.180.12.3026-3030.1998.

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