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A Trypanosoma brucei gene family encoding protein kinases with catalytic domains structurally related to Nek1 and NIMA.
Title | A Trypanosoma brucei gene family encoding protein kinases with catalytic domains structurally related to Nek1 and NIMA. |
Publication Type | Journal Article |
Year of Publication | 1993 |
Authors | Gale, M, Parsons, M |
Journal | Mol Biochem Parasitol |
Volume | 59 |
Issue | 1 |
Pagination | 111-21 |
Date Published | 1993 May |
ISSN | 0166-6851 |
Keywords | Alleles, 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 Journal | Mol. Biochem. Parasitol. |
PubMed ID | 8515773 |