Access Type

Open Access Thesis

Date of Award

January 2013

Degree Type

Thesis

Degree Name

M.S.

Department

Biochemistry and Molecular Biology

First Advisor

TIMOTHY L. STEMMLER

Abstract

ABSTRACT

Cysteine desulfurase and Isd11: A Drosophila model

Iron-sulfur clusters are cofactors with evolutionary origins that date back to the pre-biotic world. Ever since life originated, these cofactors have intermingled with proteins to play vital roles in sustaining life. My research focuses on one such protein, the cysteine desulfurase (Nfs) that has the PLP cofactor incorporated in its active site and avails of the catalytic property of PLP to provide sulphur for Iron-sulfur cluster biogenesis and assembly in a cell. Interestingly, in a eukaryotic cell, despite the versatility of PLP, cysteine desulfurase's role as a "sulphur-extractor" is incomplete without another protein named Isd11. This interesting piece of evidence led us to perform basic protein characterisation of both the proteins so as to biophysically study the binding event and conformational changes during persulfide formation in future. We chose Drosophila as our model organism. We have been able to successfully create a working model for further characterisation of the binding event during persulfide formation and also, study the complexation event involving all Iron-sulfur cluster biogenesis assembly proteins during 2Fe-2S cluster formation.

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