Plasmodium berghei, P. chabaudi, and P. falciparum: Similarities in phosphoproteins and protein kinase activities and their stage specific expression

Wiser, Mark F.; Plitt, Brigitte

doi:10.1016/0014-4894(87)90043-9

Cited by 30 publications

(21 citation statements)

References 13 publications

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“…In brief, the activity phosphorylated casein as well as phosvitin, required Mg 2ϩ , preferred ATP over GTP, was stimulated by polyamines spermine and spermidine, and was inhibited by the flavone, quercitin. It also appeared that trophozoites possessed higher amounts of this activity than either the ring or schizont stages (30), which is similar to the stage-specific variation of PfCK1 activity that we have observed (Figs. 6 and 7).…”

Section: Discussionsupporting

confidence: 87%

“…7). However, the possibility that some substrate proteins themselves may also undergo stage-specific expression has been suggested (30) and merits further investigation for its obvious regulatory implications. In recent years, Plasmodium infection of human red blood cells was shown to result in elevated phosphorylation of a number of human red blood cell membrane proteins (38 -41).…”

Section: Discussionmentioning

confidence: 99%

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Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

Barik

Taylor

Chakrabarti

1997

Journal of Biological Chemistry

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The cDNA for casein kinase 1 (CK1) of Plasmodium falciparum was cloned, sequenced, and expressed in bacteria. The single major open reading frame of the 1.2-kilobase pair cDNA coded for a 324-amino acid polypeptide of ϳ37 kDa, the predicted sequence of which showed strong identity with known CK1 isoforms. The purified recombinant enzyme exhibited properties characteristic of CK1, such as inhibition by CK1-7, the ability to phosphorylate a highly specific peptide substrate, and a strong preference for ATP over GTP. A casein kinase activity, partially purified from soluble extracts of P. falciparum by affinity chromatography through CK1-7 columns displayed identical properties. The activity showed a stage-specific expression in the parasite, in the order trophozoite > ring > > schizont. Northern analysis indicated the existence of two major CK1 mRNAs, 2.4 and 3.2 kilobase pairs long, the levels of which were in the order ring > schizont > trophozoite. Mutagenesis of recombinant CK1 defined important amino acid residues and their potential role in the conformation of the enzyme. The malarial CK1 appeared to be the one of the smallest and perhaps the most primitive CK1 enzymes known, containing little sequence information beyond the minimal catalytic domain.The parasitic protozoan, Plasmodium falciparum, is the causative agent of malaria throughout the world and is responsible for an annual death toll of nearly 3 million, the majority of which are children and pregnant mothers (1). However, tools available to control malaria are inadequate, and drug-resistant strains are widespread; moreover, the immediate prospect of a useful vaccine is uncertain. Thus, there is an urgent need to obtain fundamental knowledge about the various cellular processes of P. falciparum at the molecular level, so that susceptible targets can be identified. With this long-term goal in mind, we have initiated studies of the signal transduction system in P. falciparum. Since reversible protein phosphorylation and dephosphorylation constitute a major mechanism of signal transduction (2), one of our immediate goals has been to characterize the various protein kinases in P. falciparum. In this paper, we report the characterization, expression, stagespecific regulation, and mutational analysis of P. falciparum casein kinase 1 (PfCK1). 1 Casein kinase-1 and -2 (CK1 and CK2) are multipotential Ser/Thr protein kinases, originally purified from rabbit reticulocyte lysates using casein as substrate (reviewed in Refs. 3 and 4). In the subsequent years, both enzymes were shown to phosphorylate, and thus regulate, a wide variety of cellular proteins. The sequence alignment of CK1 genes of various organisms and deletion analysis of recombinant yeast CK1 have recently resulted in the delineation of the following domains in the prototype 45-kDa yeast enzyme (summarized in Refs. 5 and 6): an N-terminal catalytic domain of about 300 amino acids followed by a 12-residue stretch conserved among some forms but not in others; a hydrophilic 85-residue segment predi...

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

Barik

Taylor

Chakrabarti

1997

Journal of Biological Chemistry

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“…Parasites were isolated by differential centrifugation following two rounds of lysis with 0.01% saponin and washed with K-1 buffer until hemoglobin free as described [23]. The packed parasites were either immediately extracted for DNA or stored at − 75°C until use.…”

Section: Parasitesmentioning

confidence: 99%

The complete sequence of Plasmodium berghei merozoite surface protein-1 and its inter- and intra-species variability

Jennings

Toebe

Belkum

et al. 1998

Molecular and Biochemical Parasitology

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The complete gene for merozoite surface protein-1 (MSP-1) from Plasmodium berghei has been cloned and sequenced. Comparison of the P. berghei MSP-1 sequence with MSP-1 from other rodent parasites reveals five conserved domains interrupted by four variable blocks. These variable blocks exhibit no sequence homology but do have similar amino acid compositions. Primary proteolytic processing sites are located near the boundaries between the conserved domains and the variable blocks. Sequencing of the variable blocks from several P. berghei isolates shows that the predominant intra-species difference is in the number of tandem repeats. The inter-and intra-species differences suggest that the variable blocks are localized areas with relatively high levels of slipped-strand mispairing, unequal crossing-over, or other intragenic recombination activity. MSP-1 from P. berghei exhibits more repetitiveness than MSP-1 from other species suggesting that P. berghei experiences a higher intrinsic level of events producing variable numbers of tandem repeats or a lower level of events leading to the degeneration of tandem repeats.

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“…Pfp23 was initially identified as a 36-kDa major phosphoprotein associated with the kinase activity of an unknown protein in P. falciparum [21,22]. Subsequent procurement of its protein sequence revealed its homology to the co-chaperone p23 [20].…”

Section: Introductionmentioning

confidence: 99%

Characterization of Plasmodium falciparum co-chaperone p23: its intrinsic chaperone activity and interaction with Hsp90

Chua

Low²,

Goo³

et al. 2010

Cell. Mol. Life Sci.

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It is well known that the co-chaperone p23 regulates Hsp90 chaperone activity in protein folding. In Plasmodium falciparum, a putative p23 (Pfp23) has been identified through genome analysis, but its authenticity has remained unconfirmed since co-immunoprecipitation experiments failed to show its interaction with P. falciparum Hsp90 (PfHsp90). Thus, recombinant Pfp23 and PfHsp90 proteins purified from expressed clones were used in this study. It was clear that Pfp23 exhibited chaperone activity by virtue of its ability to suppress citrate synthase aggregation at 45 degrees C. Pfp23 was also shown to interact with PfHsp90 and to suppress its ATPase activity. Analyses of modeled Pfp23-PfHsp90 protein complex and site-directed mutagenesis further revealed strategically placed amino acid residues, K91, H93, W94 and K96, in Pfp23 to be crucial for binding PfHsp90. Collectively, this study has provided experimental evidence for the inherent chaperone function of Pfp23 and its interaction with PfHsp90, a sequel widely required for client protein activation.

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Plasmodium berghei, P. chabaudi, and P. falciparum: Similarities in phosphoproteins and protein kinase activities and their stage specific expression

Cited by 30 publications

References 13 publications

Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

The complete sequence of Plasmodium berghei merozoite surface protein-1 and its inter- and intra-species variability

Characterization of Plasmodium falciparum co-chaperone p23: its intrinsic chaperone activity and interaction with Hsp90

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