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

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    Author(s)
    Zalucki, Yaramah M
    Power, Peter M
    Jennings, Michael P
    Griffith University Author(s)
    Jennings, Michael P.
    Zalucki, Yaramah
    Year published
    2007
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    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 ...
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    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 aminopeptidase (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.
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    Journal Title
    Nucleic Acids Research
    Volume
    35
    Issue
    17
    DOI
    https://doi.org/10.1093/nar/gkm577
    Copyright Statement
    © 2007 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
    Subject
    Protein Trafficking
    Environmental Sciences
    Biological Sciences
    Information and Computing Sciences
    Publication URI
    http://hdl.handle.net/10072/159524
    Collection
    • Journal articles

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