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

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.

Grantor dc:publisher

Wake Forest University

Year dc:date.issued

2019

Author dc:creator

• Zheng, Chenkang

• bacteria

Language dc:language.iso

en

Handle dc:identifier.uri

http://hdl.handle.net/10339/93918

OAI identifier oai:identifier

oai:wakespace.lib.wfu.edu:10339/93918