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The Toxoplasma gondii plastid replication and repair enzyme Complex, PREX

Mukhopadhay, A. and Chen, C.Y and Doerig, C. and Henriquez, F.L. and Roberts, C.W. and Barrett, M.P. (2009) The Toxoplasma gondii plastid replication and repair enzyme Complex, PREX. Parasitology, 136 (7). pp. 747-755. ISSN 0031-1820

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Abstract

A plastid-like organelle, the apicoplast, is essential to the majority of medically and veterinary important apicomplexan protozoa including Toxoplasma gondii and Plasmodium. The apicoplast contains multiple copies of a 35 kb genome, the replication of which is dependent upon nuclear-encoded proteins that are imported into the organelle. In P. falciparum an unusual multi-functional gene, pfprex, was previously identified and inferred to encode a protein with DNA primase, DNA helicase and DNA polymerase activities. Herein, we report the presence of a prex orthologue in T. gondii. The protein is predicted to have a bi-partite apicoplast targeting sequence similar to that demonstrated on the PfPREX polypeptide, capable of delivering marker proteins to the apicoplast. Unlike the P. falciparum gene that is devoid of introns, the T. gondii prex gene carries 19 introns, which are spliced to produce a contiguous mRNA. Bacterial expression of the polymerase domain reveals the protein to be active. Consistent with the reported absence of a plastid in Cryptosporidium species, in silico analysis of their genomes failed to demonstrate an orthologue of prex. These studies indicate that prex is conserved across the plastid-bearing apicomplexans and may play an important role in the replication of the plastid genome.

Item type: Article
ID code: 15304
Keywords: Apicomplexa, DNA replication, Plasmodium falciparum, Toxoplasma gondii, exon, intron, DNA polymerase, DNA primase, DNA helicase, Therapeutics. Pharmacology, Pharmacy and materia medica, Microbiology
Subjects: Medicine > Therapeutics. Pharmacology
Medicine > Pharmacy and materia medica
Science > Microbiology
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Faculty of Engineering > Chemical and Process Engineering
Faculty of Science > Immunology
Related URLs:
    Depositing user: Ms Ann Barker-Myles
    Date Deposited: 05 Feb 2010 16:11
    Last modified: 12 Mar 2012 11:01
    URI: http://strathprints.strath.ac.uk/id/eprint/15304

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