The University of St Andrews

Research@StAndrews:FullText >
University of St Andrews Research >
University of St Andrews Research >
University of St Andrews Research >

Please use this identifier to cite or link to this item:
This item has been viewed 6 times in the last year. View Statistics

Files in This Item:

File Description SizeFormat
MacqueenJohnstonBMCEvolBiol1471_2148_9_34Akiringenefamily.pdf3.65 MBAdobe PDFView/Open
Title: Evolution of the multifaceted eukaryotic akirin gene family
Authors: Macqueen, Daniel J.
Johnston, Ian A.
Keywords: NF-KAPPA-B
Genome duplication
Functional divergence
Phylogenetic analysis
Sequence alignments
Nuclear export
2 rounds
QH426 Genetics
Issue Date: 6-Feb-2009
Citation: Macqueen , D J & Johnston , I A 2009 , ' Evolution of the multifaceted eukaryotic akirin gene family ' BMC Evolutionary Biology , vol 9 , 34 . , 10.1186/1471-2148-9-34
Abstract: Background: Akirins are nuclear proteins that form part of an innate immune response pathway conserved in Drosophila and mice. This studies aim was to characterise the evolution of akirin gene structure and protein function in the eukaryotes. Results: akirin genes are present throughout the metazoa and arose before the separation of animal, plant and fungi lineages. Using comprehensive phylogenetic analysis, coupled with comparisons of conserved synteny and genomic organisation, we show that the intron-exon structure of metazoan akirin genes was established prior to the bilateria and that a single proto-orthologue duplicated in the vertebrates, before the gnathostome-agnathan separation, producing akirin1 and akirin2. Phylogenetic analyses of seven vertebrate gene families with members in chromosomal proximity to both akirin1 and akirin2 were compatible with a common duplication event affecting the genomic neighbourhood of the akirin proto-orthologue. A further duplication of akirins occurred in the teleost lineage and was followed by lineage-specific patterns of paralogue loss. Remarkably, akirins have been independently characterised by five research groups under different aliases and a comparison of the available literature revealed diverse functions, generally in regulating gene expression. For example, akirin was characterised in arthropods as subolesin, an important growth factor and in Drosophila as bhringi, which has an essential myogenic role. In vertebrates, akirin1 was named mighty in mice and was shown to regulate myogenesis, whereas akirin2 was characterised as FB11 in rats and promoted carcinogenesis, acting as a transcriptional repressor when bound to a 14-3-3 protein. Both vertebrate Akirins have evolved under comparably strict constraints of purifying selection, although a likelihood ratio test predicted that functional divergence has occurred between paralogues. Bayesian and maximum likelihood tests identified amino-acid positions where the rate of evolution had shifted significantly between paralogues. Interestingly, the highest scoring position was within a conserved, validated binding-site for 14-3-3 proteins. Conclusion: This work offers an evolutionary framework to facilitate future studies of eukaryotic akirins and provides insight into their multifaceted and conserved biochemical functions.
Version: Publisher PDF
Status: Peer reviewed
ISSN: 1471-2148
Type: Journal article
Rights: © 2009 Macqueen and Johnston; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Appears in Collections:Scottish Oceans Institute Research
Centre for Research into Ecological & Environmental Modelling (CREEM) Research
Biology Research
University of St Andrews Research

This item is protected by original copyright

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.


DSpace Software Copyright © 2002-2012  Duraspace - Feedback
For help contact: | Copyright for this page belongs to St Andrews University Library | Terms and Conditions (Cookies)