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MBE Advance Access originally published online on December 23, 2003
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Mol. Biol. Evol. 21(3):489-497. 2004
DOI: 10.1093/molbev/msh042
© 2004 by the Society for Molecular Biology and Evolution. ISSN: 0737-4038

Evolution of Cryptosporidium parvum Lactate Dehydrogenase from Malate Dehydrogenase by a Very Recent Event of Gene Duplication

Dominique Madern*, Xiaomin Cai{dagger}, Mitchell S. Abrahamsen{ddagger} and Guan Zhu{dagger}

* Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale CEA-CNRS-UJF, Grenoble, France
{dagger} Department of Veterinary Pathobiology, Texas A&M University, College Station
{ddagger} Department of Veterinary Pathobiology, University of Minnesota, St. Paul

E-mail: g3hu{at}cvm.tamu.edu.

We have expressed the L-lactate dehydrogenase (LDH) and L-malate dehydrogenase (malDH) genes from the apicomplexan Cryptosporidium parvum (CpLDH1 and CpMalDH1) as maltose-binding protein (MBP) fusion proteins in Escherichia coli. The substrate specificities, enzymatic kinetics, and oligomeric states of these two parasite enzymes have been characterized. By taking advantage of recently completed and ongoing apicomplexan genome sequencing projects, we identified additional MalDH genes from Plasmodium spp., Toxoplasma gondii, and Eimeria tenella that were previously unavailable. All apicomplexan MalDHs appeared to be cytosolic and no organellar homologs were identified from the completely sequenced P. falciparum genome and other ongoing apicomplexan genome-sequencing projects. Using these expanded apicomplexan LDH and MalDH sequence databases, we reexamined their phylogenetic relationships and reconfirmed their relationship to {alpha}-proteobacterial MalDHs. All LDH and MalDH enzymes from apicomplexans were monophyletic within the LDH-like MalDH group (i.e., MalDH resembling LDH) as a sister to {alpha}-proteobacterial MalDHs. All apicomplexan LDHs, with the exception of CpLDH1, formed a separate clade from their MalDH counterparts, indicating that these LDHs were evolved from an ancestral apicomplexan MalDH by a gene duplication coupled with functional conversion before the expansion of apicomplexans. Finally, CpLDH1 was consistently placed together with CpMalDH1 within the apicomplexan MalDH cluster, confirming an early working hypothesis that CpLDH1 was probably evolved from the same ancestor of CpMalDH1 by a very recent gene duplication that occurred after C. parvum diverged from other apicomplexans.

Key Words: Apicomplexa • Cryptosporidium parvum • malate dehydrogenase • lactate dehydrogenase • phylogeny • evolution • gene duplication


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