Two proteins involved in kinetoplast compaction.
The kinetoplast is the genome of the single mitochondrion of trypanosomatid Protozoa, and contains up to 30% of total cellular DNA in a network of catenated AT-rich rings. EM studies show that the kinetoplast is organized into a compact, disc-shaped structure in vivo, but little is known about proteins involved in its architecture. Defining such proteins would be useful to understand the molecular biology of this unusual organelle and to design compounds to contain parasite growth. We show here that two proteins, p1 and p2 of M(r) approximately 22 and approximately 21 kDa, respectively, from the trypanosomatid Crithidia fasciculata can compact kDNA networks efficiently in vitro, the first such demonstration with purified trypanosome proteins. We show that these proteins are localized exclusively in the parasite's kinetoplast. Our data thus define two proteins potentially involved in kinetoplast organization in vivo.
Tittawella
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Department of Cell and Molecular Biology, University of Umeå, Sweden.
Carlsson
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Thornell
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D000818:Animals; D015153:Blotting, Western; D016831:Crithidia fasciculata / Q000235:genetics / Q000378:metabolism*; D018105:DNA, Kinetoplast / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D009690:Nucleic Acid Conformation; D015800:Protozoan Proteins / Q000378:metabolism*
D018105:DNA, Kinetoplast; D004268:DNA-Binding Proteins; D015800:Protozoan Proteins