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A Trypanosoma brucei gene family encoding protein kinases with catalytic domains structurally related to Nek1 and NIMA.

TitleA Trypanosoma brucei gene family encoding protein kinases with catalytic domains structurally related to Nek1 and NIMA.
Publication TypeJournal Article
Year of Publication1993
AuthorsGale, M, Parsons, M
JournalMol Biochem Parasitol
Volume59
Issue1
Pagination111-21
Date Published1993 May
ISSN0166-6851
KeywordsAlleles, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Protozoan, Genes, Protozoan, Mice, Molecular Sequence Data, Multigene Family, Phosphorylation, Protein Kinases, Restriction Mapping, Sequence Homology, Amino Acid, Trypanosoma brucei brucei
Abstract

Using polymerase chain reaction technology we cloned a Trypanosoma brucei gene fragment that has a deduced amino acid sequence with a high degree of homology to protein kinase catalytic domains. This clone detects two genes by genomic Southern analysis. These genes, nrkA and nrkB, share a 97% nt sequence homology over their 1.3-kb coding regions. NrkA encodes a 48-kDa protein which possess all 11 protein kinase homology regions. The 279-aa N-terminal catalytic domain has highest homology with Nek1, a bifunctional kinase, and NIMA, a protein serine/threonine kinase. Both alleles at the nrkB locus in T. brucei strain IsTAR 1 encode a truncated protein kinase catalytic domain due the presence of a premature termination codon. However, the TREU667 strain is heterozygous at the nrkB locus, encoding one truncated and one full-length molecule. NrkA and NrkB possess multiple phosphorylation site motifs. Both nrk transcripts are constitutively expressed during parasite development.

Alternate JournalMol. Biochem. Parasitol.
PubMed ID8515773