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Plasmodium falciparummyosins: Transcription and translation during asexual parasite development


Reference:

Chaparro-Olaya, J., Margos, G., Coles, D. J., Dluzewski, A. R., Mitchell, G. H., Wasserman, M. M. and Pinder, J. C., 2005. Plasmodium falciparummyosins: Transcription and translation during asexual parasite development. Cell Motility and the Cytoskeleton, 60 (4), pp. 200-213.

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Official URL:

http://dx.doi.org/10.1002/cm.20055

Abstract

Six myosins genes are now annotated in the Plasmodium falciparum Genome Project. Malaria myosins have been named alphabetically; accordingly, we refer to the two latest additions as Pfmyo-E and Pfmyo-F. Both new myosins contain regions characteristic of the functional motor domain of “true” myosins and, unusually for P. falciparum myosins, Pfmyo-F encodes two consensus IQ light chain-binding motifs. Phylogenetic analysis of the 17 currently known apicomplexan myosins together with one representative of each myosin class clusters all but one of the apicomplexan sequences together in Class XIV. This refines the earlier definition of the Class XIV Subclasses XIVa and XIVb. RT-PCR on blood stage parasite mRNA amplifies a specific product for all six myosins and each shows developmentally regulated transcription. Thus: Pfmyo-A and Pfmyo-B genes are transcribed throughout development; Pfmyo-C is predominant in trophozoites; Pfmyo-D occurs in trophozoites and schizonts; Pfmyo-E though barely present in earlier stages is abundant in schizonts; Pfmyo-F increases steadily throughout development and maturation. It is known that Pfmyo-A and Pfmyo-B are synthesised during late schizogony and we now show that Pfmyo-D expression is also temporally regulated to late trophozoites and schizonts where it distributes close to segregating nuclei. Thus, in asexual stages myosin synthesis does not always parallel transcript accumulation, showing that translation is also regulated. The implication is that the mRNAs are either subjected to turnover, synthesised and degraded, or that they are sequestered in an inactivate form until required for protein synthesis.

Details

Item Type Articles
CreatorsChaparro-Olaya, J., Margos, G., Coles, D. J., Dluzewski, A. R., Mitchell, G. H., Wasserman, M. M. and Pinder, J. C.
DOI10.1002/cm.20055
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code28629

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