Primary structure and sexual stage-specific expression of a LAMMER protein kinase of Plasmodium falciparum.

JLLi; GATargett; DA Baker ORCID logo; (2001) Primary structure and sexual stage-specific expression of a LAMMER protein kinase of Plasmodium falciparum. International journal for parasitology, 31 (4). pp. 387-392. ISSN 0020-7519 DOI: 10.1016/s0020-7519(01)00126-6
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We have isolated a LAMMER-like gene from Plasmodium falciparum by vectorette technique. The gene consists of 3316 bp encoding a protein 881 amino acids with a predicted molecular mass of approximately 106.7 kDa. The encoded protein, termed PfLAMMER, is composed of two distinct domains. The N-terminal domain is not related to any previously described protein kinases and has several interesting features including multiple consensus phosphorylation sites for a range of protein kinases, a number of RS/SR dipeptides, a large proportion of charged amino acids, two putative nuclear localisation signals and 14 copies of a tetramer DKYD repeats. The C-terminal domain is characteristic of a kinase in the LAMMER family with the highest homology to the Arabidopsis thaliana AFC3 kinase. Genomic restriction analysis showed that PfLAMMER is encoded by a single copy gene in the parasite genome. A single transcript of approximately 3800 nucleotides is expressed specifically in the sexual stage, indicating that PfLAMMER may be important in regulating the processes of sexual differentiation of the parasite.


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