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Abbreviated Journal Title

J. Biol. Chem.

Keywords

Directed Protein-Kinase; Erythrocyte-Membrane; Molecular-Cloning; Surface-Antigen; Phosphorylation; Yeast; Purification; Sequence; Cell; Phosphoproteins; Biochemistry & Molecular Biology

Abstract

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 similar to 37 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 much greater than schizont. Northern analysis indicated the existence of two major CK1 mRNAs, 2.4 and 3.2 kilobase pairs long, the levels of which mere 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.

Journal Title

Journal of Biological Chemistry

Volume

272

Issue/Number

42

Publication Date

1-1-1997

Document Type

Article

Language

English

First Page

26132

Last Page

26138

WOS Identifier

WOS:A1997XR27100041

ISSN

0021-9258

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