Identification of pentatricopeptide repeat proteins in Trypanosoma brucei

Mol Biochem Parasitol. 2006 Nov;150(1):37-45. doi: 10.1016/j.molbiopara.2006.06.006. Epub 2006 Jun 28.


A new class of organellar proteins, characterized by pentatricopeptide repeat (PPR) motifs, has been identified in plants. These proteins contain multiple 35-amino acid repeats that are proposed to form a super helix capable of binding a strand of RNA. All PPR proteins characterized to date appear to be involved in RNA processing pathways in organelles. Twenty-three PPR proteins have been identified in Trypanosoma brucei and database research indicates that most of these proteins are predicted to contain the traditional mitochondrial target sequence. Orthologues of each of the 23 proteins have also been identified in Leishmania major and Trypanosoma cruzi, indicating that these proteins represent a highly conserved class of proteins within the kinetoplastid family. Preliminary experiments using RNAi to specifically silence one identified PPR gene (TbPPRl- Tb927.2.3180), indicate that cells depleted of TbPPRl transcripts show a slow growth phenotype and altered mitochondrial maxicircle RNA profiles. This initial characterization suggests that PPR proteins will play important roles in the complex RNA processing required for mitochondrial gene expression in trypanosomes.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Blotting, Northern
  • Gene Expression Regulation
  • Mitochondria / genetics
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / genetics
  • RNA Interference
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • Transfection
  • Trypanosoma brucei brucei / chemistry*
  • Trypanosoma brucei brucei / genetics


  • Protozoan Proteins
  • RNA-Binding Proteins