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dc.contributor.authorM. Zalucki, Yaramahen_US
dc.contributor.authorM. Power, Peteren_US
dc.contributor.authorP. Jennings, Michaelen_US
dc.description.abstractThe 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.en_US
dc.publisherOxford University Pressen_US
dc.publisher.placeUnited Kingdomen_US
dc.relation.ispartofjournalNucleic Acids Researchen_US
dc.subject.fieldofresearchProtein Traffickingen_US
dc.titleSelection for efficient translation initiation biases codon usage at second amino acid position in secretory proteinsen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.hasfulltextNo Full Text

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