Open AccessTcDJ1, a putative mitochondrial DnaJ protein in Trypanosoma cruzi 1
Author(s) -
Carreira Mônica A.C,
Tibbetts Randal S,
Olson Cheryl L,
Schuster Cristoph,
Renz Manfred,
Engman David M,
Goldenberg Samuel
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13195.x
Subject(s) - trypanosoma cruzi , biology , complementary dna , biochemistry , microbiology and biotechnology , amino acid , zinc finger , cdna library , peptide sequence , gene , parasite hosting , world wide web , computer science , transcription factor
A full length cDNA encoding a novel Trypanosoma cruzi DnaJ protein was cloned and characterized. The 324 amino acid protein encoded by the cDNA (TcDJ1) displays a characteristic J‐domain, but lacks the Gly‐Phe and zinc finger regions present in some other DnaJ proteins. Relative to four other T. cruzi DnaJ proteins, TcDJ1 has an amino terminal extension containing basic and hydroxylated residues characteristic of mitochondrial import peptides. A T. cruzi transfectant expressing epitope‐tagged TcDJ1 was generated and subcellular fractions were produced. Western blot analysis revealed that the protein has a molecular mass of 29 kDa and is found in the mitochondrial fraction. The expression of TcDJ1 is developmentally regulated since the levels of both mRNA and protein are much higher in epimastigotes (replicative form) than in metacyclic trypomastigotes (infective form). Thus it may participate in mitochondrial biosynthetic processes in this organism.