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Coupling between codon usage, translation and protein export in Escherichia coli
Author(s) -
Zalucki Yaramah M.,
Beacham Ifor R.,
Jennings Michael P.
Publication year - 2011
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201000334
Subject(s) - periplasmic space , signal peptide , signal recognition particle , secretory protein , cytoplasm , protein folding , microbiology and biotechnology , secretory pathway , biology , native state , biochemistry , protein sorting signals , biophysics , chemistry , secretion , peptide sequence , escherichia coli , endoplasmic reticulum , gene , golgi apparatus
Proteins destined for export via the Sec‐dependent pathway are synthesized with a short N‐terminal signal peptide. A requirement for export is that the proteins are in a translocationally competent state. This is a loosely folded state that allows the protein to pass through the SecYEG apparatus and pass into the periplasm. In order to maintain pre‐secretory proteins in an export‐competent state, there are many factors that slow the folding of the pre‐secretory protein in the cytoplasm. These include cytoplasmic chaperones, such as SecB, and the signal recognition particle, which bind the pre‐secretory protein and direct it to the cytoplasmic membrane for export. Recently, evidence has been published that non‐optimal codons in the signal sequence are important for a time‐critical early event to allow the correct folding of pre‐secretory proteins. This review details the recent developments in folding of the signal peptide and the pre‐secretory protein.