Stage specific kinetoplast DNA-binding proteins in Trypanosoma cruzi

Knowledge regarding kinetoplast DNA organization in all members of the Trypanosomatid family is incomplete. Recently, the presence of kinetoplast-associated proteins in condensing kDNA networks in Crithidia fasciculata has been described and a role for these proteins in the maintenance of these comp...

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Bibliographic Details
Published in:Acta tropica 2000-09, Vol.76 (2), p.139-146
Main Authors: Zavala-Castro, Jorge E, Acosta-Viana, Karla, Guzmán-Marı́n, Eugenia, Rosado-Barrera, Marı́a Eugenia, Rosales-Encina, José Luis
Format: Article
Language:English
Subjects:
Animals
Bacterial Proteins
Biological and medical sciences
Blotting, Western
Deoxyribonucleases, Type II Site-Specific - chemistry
DNA organization
DNA Probes - chemistry
DNA, Kinetoplast - chemistry
DNA, Kinetoplast - isolation & purification
DNA-Binding Proteins - chemistry
Electrophoresis, Polyacrylamide Gel
Human protozoal diseases
Humans
Infectious diseases
Kinetoplast DNA-binding proteins
Medical sciences
Mitochondrial DNA
Parasitic diseases
Protozoal diseases
Protozoan Proteins - chemistry
Tropical medicine
Trypanosoma cruzi
Trypanosoma cruzi - chemistry
Trypanosoma cruzi - genetics
Trypanosomiasis
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Summary:Knowledge regarding kinetoplast DNA organization in all members of the Trypanosomatid family is incomplete. Recently, the presence of kinetoplast-associated proteins in condensing kDNA networks in Crithidia fasciculata has been described and a role for these proteins in the maintenance of these complex structures was suggested. To investigate the presence of protein components in Trypanosoma cruzi kinetoplast, we previously described seven epimastigote kinetoplast-associated proteins. We report here the existence of kinetoplast binding proteins in amastigote and trypomastigote stages of T. cruzi, which could bind both mini and maxicircles components with a stage specific elements for every infective form of the parasite. We propose three major classes of kinetoplast-associated proteins related to the basic processes of this intricate disc structure and suggest a possible function of these binding proteins in the T. cruzi mitochondrial DNA organization.
ISSN:0001-706X
1873-6254
DOI:10.1016/S0001-706X(00)00079-6