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Research Article

Complete Inventory of ABC Proteins in Human Pathogenic Yeast, Candida albicans

Gaur M.a · Choudhury D.b · Prasad R.a

Author affiliations

aSchool of Life Sciences, and bCenter for Biotechnology, Jawaharlal Nehru University, New Delhi, India

Related Articles for ""

J Mol Microbiol Biotechnol 2005;9:3–15

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Article / Publication Details

First-Page Preview
Abstract of Research Article

Published online: October 28, 2005
Issue release date: October 2005

Number of Print Pages: 13
Number of Figures: 2
Number of Tables: 3

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB

Abstract

The recent completion of the sequencing project of the opportunistic human pathogenic yeast, Candida albicans (http://www.ncbi.nlm.nih.gov/), led us to analyze and classify its ATP-binding cassette (ABC) proteins, which constitute one of the largest superfamilies of proteins. Some of its members are multidrug transporters responsible for the commonly encountered problem of antifungal resistance. TBLASTN searches together with domain analysis identified 81 nucleotide-binding domains, which belong to 51 different putative open reading frames. Considering that each allelic pair represents a single ABC protein of the Candida genome, the total number of putative members of this superfamily is 28. Domain organization, sequence-based analysis and self-organizing map-based clustering led to the classification of Candida ABC proteins into 6 distinct subfamilies. Each subfamily from C. albicans has an equivalent in Saccharomyces cerevisiae suggesting a close evolutionary relationship between the two yeasts. Our searches also led to the identification of a new motif to each subfamily in Candida that could be used to identify sequences from the corresponding subfamily in other organisms. It is hoped that the inventory of Candida ABC transporters thus created will provide new insights into the role of ABC proteins in antifungal resistance as well as help in the functional characterization of the superfamily of these proteins.

© 2005 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Research Article

Published online: October 28, 2005
Issue release date: October 2005

Number of Print Pages: 13
Number of Figures: 2
Number of Tables: 3

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB


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