Cloning and characterization of the casein kinase II α subunit gene from the lymphocyte-transforming intracellular protozoan parasite theileria parva

Onesmo K. Ole-MoiYoi, Chihiro Sugimoto, Patricia A Conrad, Michael D. Macklin

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Theileria parva is an obligate intracellular protozoan parasite which is the causative agent of East Coast fever, an acute, leukemia-like disease of cattle. The intralymphocytic stage of the parasite induces blastogenesis and clonal expansion of quiescent bovid lymphocytes. Experiments in our laboratory have shown a marked increase of casein kinase II- (CK II-) like activity in T. parva-transformed lymphocytes. We have also detected CK II activity in purified T. parva schizonts. To explore the significance of this increase, we used a Drosophila melanogaster CK II α cDNA probe [Saxena et al. (1987) Mol. Cell Biol. 7, 3409-3417] to isolate a T. parva genomic clone encoding a CK II catalytic subunit. The clone contains a 1.3-kb open reading frame coding for a predicted protein of 420 amino acids (Mr 50 200). Northern blot analysis revealed a single transcript of 1.65 kb. The deduced T. parva CK II catalytic subunit sequence shows, over 321 residues comprising the C-terminus of the molecule, extensive identity with CK II α and α′ sequences from both vertebrate and invertebrate organisms. The T. parva CK II subunit amino acid sequence displays 68% identity with the Drosophila a subunit and 67% with the Caenorhabditis elegans a subunit but only 58% and 56% sequence identity with the Saccharomyces cerevisiae α and α′ subunits, respectively. Comparison of the T. parva sequence with higher eukaryotic α and α′ sequences reveals that it is most identical with the α subunit. A unique component of the T. parva CK II α subunit is a 99 amino acid sequence at the N-terminus, which contains a sequence motif with features characteristic of signal peptides.

Original languageEnglish (US)
Pages (from-to)6193-6202
Number of pages10
JournalBiochemistry
Volume31
Issue number27
StatePublished - 1992

Fingerprint

Theileria parva
Casein Kinase II
Lymphocytes
Cloning
Oncogenes
Organism Cloning
Parasites
Genes
Amino Acids
Protein Sorting Signals
Yeast
Coastal zones
Complementary DNA
Amino Acid Sequence
Catalytic Domain
Molecules
Clone Cells
Theileriasis
Cattle Diseases
Schizonts

ASJC Scopus subject areas

  • Biochemistry

Cite this

Cloning and characterization of the casein kinase II α subunit gene from the lymphocyte-transforming intracellular protozoan parasite theileria parva. / Ole-MoiYoi, Onesmo K.; Sugimoto, Chihiro; Conrad, Patricia A; Macklin, Michael D.

In: Biochemistry, Vol. 31, No. 27, 1992, p. 6193-6202.

Research output: Contribution to journalArticle

@article{2b021223c36f4aaf9521dec04ef91b97,
title = "Cloning and characterization of the casein kinase II α subunit gene from the lymphocyte-transforming intracellular protozoan parasite theileria parva",
abstract = "Theileria parva is an obligate intracellular protozoan parasite which is the causative agent of East Coast fever, an acute, leukemia-like disease of cattle. The intralymphocytic stage of the parasite induces blastogenesis and clonal expansion of quiescent bovid lymphocytes. Experiments in our laboratory have shown a marked increase of casein kinase II- (CK II-) like activity in T. parva-transformed lymphocytes. We have also detected CK II activity in purified T. parva schizonts. To explore the significance of this increase, we used a Drosophila melanogaster CK II α cDNA probe [Saxena et al. (1987) Mol. Cell Biol. 7, 3409-3417] to isolate a T. parva genomic clone encoding a CK II catalytic subunit. The clone contains a 1.3-kb open reading frame coding for a predicted protein of 420 amino acids (Mr 50 200). Northern blot analysis revealed a single transcript of 1.65 kb. The deduced T. parva CK II catalytic subunit sequence shows, over 321 residues comprising the C-terminus of the molecule, extensive identity with CK II α and α′ sequences from both vertebrate and invertebrate organisms. The T. parva CK II subunit amino acid sequence displays 68{\%} identity with the Drosophila a subunit and 67{\%} with the Caenorhabditis elegans a subunit but only 58{\%} and 56{\%} sequence identity with the Saccharomyces cerevisiae α and α′ subunits, respectively. Comparison of the T. parva sequence with higher eukaryotic α and α′ sequences reveals that it is most identical with the α subunit. A unique component of the T. parva CK II α subunit is a 99 amino acid sequence at the N-terminus, which contains a sequence motif with features characteristic of signal peptides.",
author = "Ole-MoiYoi, {Onesmo K.} and Chihiro Sugimoto and Conrad, {Patricia A} and Macklin, {Michael D.}",
year = "1992",
language = "English (US)",
volume = "31",
pages = "6193--6202",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "27",

}

TY - JOUR

T1 - Cloning and characterization of the casein kinase II α subunit gene from the lymphocyte-transforming intracellular protozoan parasite theileria parva

AU - Ole-MoiYoi, Onesmo K.

AU - Sugimoto, Chihiro

AU - Conrad, Patricia A

AU - Macklin, Michael D.

PY - 1992

Y1 - 1992

N2 - Theileria parva is an obligate intracellular protozoan parasite which is the causative agent of East Coast fever, an acute, leukemia-like disease of cattle. The intralymphocytic stage of the parasite induces blastogenesis and clonal expansion of quiescent bovid lymphocytes. Experiments in our laboratory have shown a marked increase of casein kinase II- (CK II-) like activity in T. parva-transformed lymphocytes. We have also detected CK II activity in purified T. parva schizonts. To explore the significance of this increase, we used a Drosophila melanogaster CK II α cDNA probe [Saxena et al. (1987) Mol. Cell Biol. 7, 3409-3417] to isolate a T. parva genomic clone encoding a CK II catalytic subunit. The clone contains a 1.3-kb open reading frame coding for a predicted protein of 420 amino acids (Mr 50 200). Northern blot analysis revealed a single transcript of 1.65 kb. The deduced T. parva CK II catalytic subunit sequence shows, over 321 residues comprising the C-terminus of the molecule, extensive identity with CK II α and α′ sequences from both vertebrate and invertebrate organisms. The T. parva CK II subunit amino acid sequence displays 68% identity with the Drosophila a subunit and 67% with the Caenorhabditis elegans a subunit but only 58% and 56% sequence identity with the Saccharomyces cerevisiae α and α′ subunits, respectively. Comparison of the T. parva sequence with higher eukaryotic α and α′ sequences reveals that it is most identical with the α subunit. A unique component of the T. parva CK II α subunit is a 99 amino acid sequence at the N-terminus, which contains a sequence motif with features characteristic of signal peptides.

AB - Theileria parva is an obligate intracellular protozoan parasite which is the causative agent of East Coast fever, an acute, leukemia-like disease of cattle. The intralymphocytic stage of the parasite induces blastogenesis and clonal expansion of quiescent bovid lymphocytes. Experiments in our laboratory have shown a marked increase of casein kinase II- (CK II-) like activity in T. parva-transformed lymphocytes. We have also detected CK II activity in purified T. parva schizonts. To explore the significance of this increase, we used a Drosophila melanogaster CK II α cDNA probe [Saxena et al. (1987) Mol. Cell Biol. 7, 3409-3417] to isolate a T. parva genomic clone encoding a CK II catalytic subunit. The clone contains a 1.3-kb open reading frame coding for a predicted protein of 420 amino acids (Mr 50 200). Northern blot analysis revealed a single transcript of 1.65 kb. The deduced T. parva CK II catalytic subunit sequence shows, over 321 residues comprising the C-terminus of the molecule, extensive identity with CK II α and α′ sequences from both vertebrate and invertebrate organisms. The T. parva CK II subunit amino acid sequence displays 68% identity with the Drosophila a subunit and 67% with the Caenorhabditis elegans a subunit but only 58% and 56% sequence identity with the Saccharomyces cerevisiae α and α′ subunits, respectively. Comparison of the T. parva sequence with higher eukaryotic α and α′ sequences reveals that it is most identical with the α subunit. A unique component of the T. parva CK II α subunit is a 99 amino acid sequence at the N-terminus, which contains a sequence motif with features characteristic of signal peptides.

UR - http://www.scopus.com/inward/record.url?scp=0026751044&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026751044&partnerID=8YFLogxK

M3 - Article

VL - 31

SP - 6193

EP - 6202

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 27

ER -