MBE Advance Access originally published online on January 22, 2004
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Mol. Biol. Evol. 21(4):632-646. 2004
DOI: 10.1093/molbev/msh054
© 2004 by the Society for Molecular Biology and Evolution. ISSN: 0737-4038
Differential Enzyme Targeting As an Evolutionary Adaptation to Herbivory in Carnivora



* Department of Biology, University College London
EM Unit, Royal Free and University College Medical School
Institute of Zoology, London, UK
Cardiff School of Biosciences, Cardiff University, Cardiff, UK
E-mail: c.danpure{at}ucl.ac.uk.
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 recognized 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 analyzed 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 toward 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
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
T. Gabaldon Peroxisome diversity and evolution Phil Trans R Soc B, March 12, 2010; 365(1541): 765 - 773. [Abstract] [Full Text] [PDF] |
||||
![]() |
Q. Han, H. Robinson, Y. G. Gao, N. Vogelaar, S. R. Wilson, M. Rizzi, and J. Li Crystal Structures of Aedes aegypti Alanine Glyoxylate Aminotransferase J. Biol. Chem., December 1, 2006; 281(48): 37175 - 37182. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. Colasante, V. P. Alibu, S. Kirchberger, J. Tjaden, C. Clayton, and F. Voncken Characterization and Developmentally Regulated Localization of the Mitochondrial Carrier Protein Homologue MCP6 from Trypanosoma brucei. Eukaryot. Cell, August 1, 2006; 5(8): 1194 - 1205. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. A. J. Huber, G. M. Birdsey, M. J. Lumb, D. T. R. Prowse, T. J. Perkins, D. R. Knight, and C. J. Danpure Peroxisomal Import of Human Alanine:glyoxylate Aminotransferase Requires Ancillary Targeting Information Remote from Its C Terminus J. Biol. Chem., July 22, 2005; 280(29): 27111 - 27120. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. M Birdsey, J. Lewin, J. D Holbrook, V. R Simpson, A. A Cunningham, and C. J Danpure A comparative analysis of the evolutionary relationship between diet and enzyme targeting in bats, marsupials and other mammals Proc R Soc B, April 22, 2005; 272(1565): 833 - 840. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. W. Jobson, R. Nielsen, L. Laakkonen, M. Wikstrom, and V. A. Albert Adaptive evolution of cytochrome c oxidase: Infrastructure for a carnivorous plant radiation PNAS, December 28, 2004; 101(52): 18064 - 18068. [Abstract] [Full Text] [PDF] |
||||




