Lack of Effect of Leader Peptidase Overproduction on the Processing in vivo of Exported Proteins in Escherichia coli
- 1 March 1986
- journal article
- research article
- Published by Microbiology Society in Microbiology
- Vol. 132 (3) , 689-696
- https://doi.org/10.1099/00221287-132-3-689
Abstract
The kinetics of maturation of certain exported proteins were analysed in Escherichia coli strains that also concomitantly overproduce either a periplasmic protein or the leader peptidase. The results led to three conclusions. (a) Overproduction of leader peptidase has no effect on the rate of maturation of at least two exported proteins, one periplasmic (TEM .beta.-lactamase), one outer membrane (PhoE); therefore, the quantity of leader peptidase is not rate-limiting for normal export. (b) Overproduction of PhoS reduces the rate of maturation of two other periplasmic proteins (.beta.-lactamase and PhoA) and itself, presumably by competing for the rate-limiting component of the export apparatus. (c) Overproduction of leader peptidase in a strain overproducing PhoS has no effect on the retarded maturation of PhoS. Therefore, even in these conditions, leader peptidase is not rate limiting.This publication has 27 references indexed in Scilit:
- A rapid boiling method for the preparation of bacterial plasmidsPublished by Elsevier ,2004
- Different exported proteins in E. coli show differences in the temporal mode of processing in vivoCell, 1981
- Assembly of Proteins into MembranesScience, 1980
- Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion.Proceedings of the National Academy of Sciences, 1980
- Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein.Journal of Biological Chemistry, 1980
- Soluble precursor of an integral membrane protein: synthesis of procoat protein in Escherichia coli infected with bacteriophage M13.Proceedings of the National Academy of Sciences, 1979
- Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322.Proceedings of the National Academy of Sciences, 1978
- Evidence for Synthesis of Alkaline Phosphatase on Membrane‐Bound Polysomes in Escherichia coliEuropean Journal of Biochemistry, 1978
- Extracellular labeling of nascent polypeptides traversing the membrane of Escherichia coli.Proceedings of the National Academy of Sciences, 1977
- Synthesis of Exported Proteins by Membrane-Bound Polysomes from Escherichia coliEuropean Journal of Biochemistry, 1977