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MBE Advance Access published online on August 29, 2003
Molecular Biology and Evolution, doi:10.1093/molbev/msg217
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2003; all rights reserved
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Accepted June 27, 2003
© 2003 Society for Molecular Biology and Evolution

Original Articles

Aspartic Proteinase Phylogeny and the Origin of Pregnancy-Associated Glycoproteins

Austin L. Hughes 1*, Jonathan A. Green 2, Helen Piontkivska 1, and R. Michael Roberts 2

1 Department of Biological Sciences, University of South Carolina, Columbia SC 29208
2 Department of Animal Science, University of Missouri-Columbia, Columbia MO 65211

* To whom correspondence should be addressed. E-mail: austin{at}biol.sc.edu.


  Abstract

The phylogenetic relationships of eukaryotic aspartic proteinases were reconstructed in order to understand the origin of pregnancy-associated glycoproteins (PAGs), which constitute a large gene family expressed in the trophoblast and placenta of mammals in the order Artiodactyla. The phylogeny supported the hypothesis that PAGs originated in mammals, being most closely related to a group of PAG-like molecules (including rodent pepsin F) found in other mammalian orders. These two groups in turn form a sister group to a group of digestive enzymes from birds and mammals, which includes pepsin A. Sequence similarity in the promoter region of artiodactyl PAGs and mouse pepsin F also supported a close relationship between these genes. Ancestral sequence reconstruction revealed that, at the residues corresponding to positions 148-150 of pepsin A, in the ancestor of artiodactyl PAGs the motif QNL was replaced by EPV; and EPV (or occasionally EPI) is conserved at these sites in known PAGs. The conservation of this ancestral change suggests that it may be important to PAG function, particularly the fact that PAGs lack proteinase activity in spite of the conservation of active site residues in most PAGs.

Key Words: aspartic proteinase, evolution of protein function, multi-gene family, pregnancy-associated glycoprotein


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[Abstract] [Full Text] [PDF]


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