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Molecular cloning of Trypanosoma brucei CK2 catalytic subunits: the alpha isoform is nucleolar and phosphorylates the nucleolar protein Nopp44/46.

Authors
  • Park, Jeong-Hyun
  • Brekken, Deirdre L
  • Randall, Amber C
  • Parsons, Marilyn
Type
Published Article
Journal
Molecular and Biochemical Parasitology
Publisher
Elsevier
Publication Date
Jan 01, 2002
Volume
119
Issue
1
Pages
97–106
Identifiers
PMID: 11755190
Source
Medline
License
Unknown

Abstract

We have demonstrated previously that Nopp44/46, an abundant nucleolar phosphoprotein of Trypanosoma brucei, is associated with a protein kinase. In many organisms multiple nucleolar proteins are phosphorylated by the protein kinase CK2, formerly known as casein kinase II. Here we report the identification of two T. brucei genes, CK2a1and CK2a2, which encode protein kinases bearing signature motifs common to CK2 catalytic subunits. The protein specified by CK2a1, designated CK2alpha, was capable of associating with Nopp44/46 as assessed by yeast two-hybrid analysis. An epitope-tagged version of CK2alpha expressed in T. brucei colocalized with Nopp44/46, with a largely nucleolar localization. This localization contrasts with the predominantly nuclear localization of mammalian CK2. When expressed in Escherichia coli, TbCK2alpha was catalytically active and phosphorylated Nopp44/46. Together these data demonstrate that TbCK2alpha is a Nopp44/46-associated kinase. Competition assays revealed that, unlike most CK2s, TbCK2alpha discriminates highly between ATP and GTP. This distinction may be associated with the substitution of glutamic acid and alanine for the di-asparagine motif thought to participate in purine interaction.

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