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MBE Advance Access published online on January 22, 2004

Molecular Biology and Evolution, doi:10.1093/molbev/msh054
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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Accepted November 4, 2003
© 2004 Society for Molecular Biology and Evolution

Original Articles

Differential Enzyme Targeting as an Evolutionary Adaptation to Herbivory in Carnivora

Graeme M. Birdsey 1, Jackie Lewin 2, Andrew A. Cunningham 3, Michael W. Bruford 4, and Christopher J. Danpure 1*

1 Department of Biology, University College London, Gower Street, London WC1E 6BT, UK
2 EM Unit, Royal Free and University College Medical School, Rowland Hill Street, London NW3 2PF, UK
3 Institute of Zoology, Regent's Park, London NW1 4RY, UK
4 Cardiff School of Biosciences, Cardiff University, Cathays Park, Cardiff CF10 3TL, UK

* To whom correspondence should be addressed. E-mail: c.danpure{at}ucl.ac.uk.


   Abstract

Not all members of the order Carnivora are carnivorous. Some are omnivorous and a few, such as the giant panda, Ailuropoda melanoleuca, are almost exclusively herbivorous. Although a number of adaptations to increased plant-eating are recognised within Carnivora, few have been studied at the molecular level. One molecular adaptation to diet that is spread widely across Mammalia is the differential intracellular targeting of the intermediary metabolic enzyme alanine:glyoxylate aminotransferase (AGT), which tends to be mitochondrial in carnivores, peroxisomal in herbivores, and both mitochondrial and peroxisomal in omnivores. In the present study, we have analysed the targeting of AGT in Carnivora in relation to species' natural diets. We show not only that there has been an adaptive shift in AGT targeting from the mitochondrion towards the peroxisome as diets have shifted from being mainly carnivorous to ones that are more omnivorous and herbivorous, but also that in one lineage, namely that of the giant panda, there is evidence for positive selection pressure at the molecular level on the AGT mitochondrial targeting sequence to decrease its efficiency, thereby allowing more AGT to be targeted to the peroxisomes.

Key Words: molecular adaptation, alanine:glyoxylate aminotransferase, dietary selection pressure, protein targeting, mitochondria, peroxisomes


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