Selection for efficient translation initiation biases codon usage at second amino acid position in secretory proteins

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Title Selection for efficient translation initiation biases codon usage at second amino acid position in secretory proteins
Author Zalucki, Yaramah M.; Power, Peter M.; Jennings, Michael Paul
Journal Name Nucleic Acids Research
Year Published 2007
Place of publication United Kingdom
Publisher Oxford University Press
Abstract The definition of a typical sec-dependent bacterial signal peptide contains a positive charge at the N-terminus, thought to be required for membrane association. In this study the amino acid distribution of all Escherichia coli secretory proteins were analysed. This revealed that there was a statistically significant bias for lysine at the second codon position (P2), consistent with a role for the positive charge in secretion. Removal of the positively charged residue P2 in two different model systems revealed that a positive charge is not required for protein export. A well-characterized feature of large amino acids like lysine at P2 is inhibition of N-terminal methionine removal by methionyl amino-peptidase (MAP). Substitution of lysine at P2 for other large or small amino acids did not affect protein export. Analysis of codon usage revealed that there was a bias for the AAA lysine codon at P2, suggesting that a non-coding function for the AAA codon may be responsible for the strong bias for lysine at P2 of secretory signal sequences. We conclude that the selection for high translation initiation efficiency maybe the selective pressure that has led to codon and consequent amino acid usage at P2 of secretory proteins.
Peer Reviewed Yes
Published Yes
Volume 35
Issue Number 17
Page from 5748
Page to 5754
ISSN 0305-1048
Date Accessioned 2010-07-21
Language en_AU
Research Centre Institute for Glycomics
Faculty Faculty of Science, Environment, Engineering and Technology
Subject Protein Trafficking
URI http://hdl.handle.net/10072/33024
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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