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Protein Specificity Dictates Proper Sulfur Transfer in the Biosynthesis of Thio-cofactors in Bacteria

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abstract
Sulfur-containing biomolecules including iron-sulfur clusters, thio-nucleosides, and other thio-cofactors are critical players in several biological processes. The sulfur element present in these molecules is predominantly originated from L-cysteine through activation by cysteine desulfurases and is relayed to specific pathways involving the synthesis of thio-cofactors. In this dissertation, we reviewed recent methods for detection and quantification of bacterial thio-nucleosides used for structural and functional studies. These approaches provide experimental tools to uncover the interconnectivity of sulfur trafficking pathways and regulatory mechanisms employed in the synthesis of thio-nucleosides and iron-sulfur clusters. This study has also surveyed distinct modes of regulation across sulfur trafficking pathways in bacteria and explored the reactivities of cysteine desulfurases from Bacillus subtilis and Azotobacter vinelandii. Despite differences in biosynthetic schemes, these pathways are controlled by specific and dynamic protein-protein interactions and dependent on the availability of reaction components including cysteine and reducing equivalents.
subject
bacteria
cysteine desulfurase
Iron-sulfur cluster
physiological reductant
thio-cofactors
thionucleosides
contributor
Zheng, Chenkang (author)
Dos Santos, Patricia C. (committee chair)
Zhang, Ke (committee member)
Alexander, Rebecca W. (committee member)
Comstock-Ferguson, Lindsay R. (committee member)
Hinze, Willie (committee member)
date
2019-05-24T08:35:36Z (accessioned)
2021-05-23T08:30:11Z (available)
2019 (issued)
degree
Chemistry (discipline)
embargo
2021-05-23 (terms)
identifier
http://hdl.handle.net/10339/93918 (uri)
language
en (iso)
publisher
Wake Forest University
title
Protein Specificity Dictates Proper Sulfur Transfer in the Biosynthesis of Thio-cofactors in Bacteria
type
Dissertation

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