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3 results on '"Rai, Versha"'

1. Characterization of Cdr1p, a major multidrug efflux protein Candida albicans: Purified protein is amenable to intrinsic fluorescence analysis

Author

Shukla, Sudhanshu, Rai, Versha, Banerjee, Dibyendu, and Prasad, Rajendra

Subjects
Candida albicans -- Genetic aspects, Drug resistance -- Research, Adenosine triphosphate -- Chemical properties, Bacterial proteins -- Chemical properties, Biological sciences, Chemistry
Abstract

A two-step purification protocol is developed using stably overexpressed His-tagged Candida drug resistance protein 1 (Cdr 1p) in Saccharomyces cerevisiae. The analysis provides a catalytically active purified ATP-binding cassette (ABC) transporter from a fungal pathogen, which is amenable to intrinsic fluorescence measurements and hence would be useful in understanding the molecular basis of antifungal transport.

Published
2006

2. Candida drug resistance protein 1, a major multidrug ATP binding cassette transporter of candida albicans, translocates fluorescent phospholipids in a reconstituted system

Author

Shukla, Sudhanshu, Rai, Versha, Saini, Preeti, Banerjee, Dibyendu, Menon, Anant K., and Prasad, Rajendra

Subjects
Binding proteins -- Structure, Cell membranes -- Research, Flow cytometry -- Analysis, Phospholipids -- Structure, Phospholipids -- Chemical properties, Biological sciences, Chemistry
Abstract

Purified candida albicans drug resistance protein 1 (Crlp), an ATP-dependent drug efflux pump is reconstituted into sealed membrane vesicles to investigate Crlp as a phospholipids translocator. Results suggest a direct link between the ability of Cdrlp to translocate fluorescent phospholipids and efllux drugs.

Published
2007

3. Functional characterization of N-terminal nucleotide binding domain (NBD-1) of a major ABC drug transporter Cdr1p of Candida albicans: Uncommon but conserved Trp326 of walker B is important for ATP binding

Author

Rai, Versha, Shukla, Sudhanshu, Jha, Sudhakar, Komath, Sneha Sudha, and Prasad, Rajendra

Subjects
Candida albicans -- Genetic aspects, Candida albicans -- Structure, Mutagenesis -- Analysis, Fluorescence spectroscopy -- Analysis, Biological sciences, Chemistry
Abstract

The relevance of the unique positioning of an atypical Trp326 residues demonstrated using purified N-terminal NBD (NBD-512) domain of Cdr1p, a major multidrug extrusion pump of human pathogenic yeast Candida albicans. A demonstration of the five Trp residues in the NBD-512 domain, Trp326 alone is important for nucleotide binding and subsequent conformational changes within the domain is presented by employing fluorescence spectroscopy, chemical modification, and site-directed mutagenesis.

Published
2005

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