HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by van der Giezen, M. Articles by Tovar, J. Search for Related Content PubMed PubMed Citation Articles by van der Giezen, M. Articles by Tovar, J. Agricola Articles by van der Giezen, M. Articles by Tovar, J.

Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica

Mark van der Giezen

Gloria León-Avila

School of Biological Sciences, Royal Holloway, University of London, Egham, Surrey TW20 0EX, UK

Correspondence
Jorge Tovar
j.tovar{at}rhul.ac.uk

Entamoeba histolytica is the causative agent of amoebiasis, a poverty-related disease that kills an estimated 100 000 people each year. E. histolytica does not contain ‘standard mitochondria’, but harbours mitochondrial remnant organelles called mitosomes. These organelles are characterized by the presence of mitochondrial chaperonin Cpn60, but little else is known about the functions and molecular composition of mitosomes. In this study, a gene encoding molecular chaperonin Cpn10 – the functional partner of Cpn60 – was cloned, and its structure and expression were characterized, as well as the cellular localization of its encoded protein. The 5' untranslated region of the gene contains all of the structural promoter elements required for transcription in this organism. The amoebic Cpn10, like Cpn60, is not significantly upregulated upon heat-shock treatment. Computer-assisted protein modelling, and specific antibodies against Cpn10 and Cpn60, suggest that both proteins interact with each other, and that they function in the same intracellular compartment. Thus, E. histolytica appears to have retained at least two of the key molecular components required for the refolding of imported mitosomal proteins.

The GenBank/EMBL/DDBJ accession number for the nucleotide sequence reported in this paper is AF513821.

Present address: School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK.

Present address: Genetics and Molecular Biology Department, CINVESTAV, IPN, Zacatenco, 07360 Mexico DF, Mexico.