Deletion of a novel protein kinase with PX and FYVE-related domains increases the rate of differentiation of Trypanosoma brucei

Mol Microbiol. 2001 Jul;41(1):33-46. doi: 10.1046/j.1365-2958.2001.02471.x.

Abstract

Growth control of African trypanosomes in the mammalian host is coupled to differentiation of a non-dividing life cycle stage, the stumpy bloodstream form. We show that a protein kinase with novel domain architecture is important for growth regulation. Zinc finger kinase (ZFK) has a kinase domain related to RAC and S6 kinases flanked by a FYVE-related zinc finger and a phox (PX) homology domain. To investigate the function of the kinase during cyclical development, a stable transformation procedure for bloodstream forms of differentiation-competent (pleomorphic) Trypanosoma brucei strains was established. Deletion of both allelic copies of ZFK by homologous recombination resulted in reduced growth of bloodstream-form parasites in culture, which was correlated with an increased rate of differentiation to the non-dividing stumpy form. Growth and differentiation rates were returned to wild-type level by ectopic ZFK expression. The phenotype is stage-specific, as growth of procyclic (insect form) trypanosomes was unaffected, and Deltazfk/Deltazfk clones were able to undergo full cyclical development in the tsetse fly vector. Deletion of ZFK in a differentiation-defective (monomorphic) strain of T. brucei did not change its growth rate in the bloodstream stage. This suggests a function of ZFK associated with the trypanosomes' decision between either cell cycle progression, as slender bloodstream form, or differentiation to the non-dividing stumpy form.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Gene Deletion*
  • Gene Expression Regulation, Developmental*
  • Humans
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / genetics*
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Structure, Tertiary
  • Protozoan Proteins*
  • Rats
  • Trypanosoma brucei brucei / enzymology
  • Trypanosoma brucei brucei / genetics
  • Trypanosoma brucei brucei / growth & development*
  • Trypanosomiasis, African / parasitology
  • Zinc Fingers

Substances

  • Protozoan Proteins
  • ZFK protein, Trypanosoma brucei
  • Protein Serine-Threonine Kinases

Associated data

  • GENBANK/AF250316