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Title page for ETD etd-08052009-165502


Type of Document Dissertation
Author Gupta, Shobhana Satyendra
Author's Email Address shobhana.s.gupta@vanderbilt.edu
URN etd-08052009-165502
Title Structural and Functional Analysis of the Helicobacter pylori Response Regulator ArsR
Degree PhD
Department Microbiology and Immunology
Advisory Committee
Advisor Name Title
Eric P. Skaar Committee Chair
Andrzej M. Krezel Committee Member
Gerald J. Stubbs Committee Member
H. Earl Ruley Committee Member
Timothy L. Cover Committee Member
Keywords
  • Helicobacter pylori
  • response regulator
Date of Defense 2009-06-05
Availability unrestricted
Abstract
The ArsRS two-component system (TCS), comprised of a sensor histidine kinase (HK) ArsS and a response regulator (RR) ArsR, contributes to pH-responsive gene regulation in Helicobacter pylori. In a typical TCS, a specific environmental stimulus triggers the HK to phosphorylate and induce a conformational change in the RR, altering its cellular functions. In order to elucidate structure-function relationships within the ArsRS TCS, we expressed and purified the full-length ArsR protein and its DNA-binding domain (ArsR-DBD), and analyzed the tertiary structure of ArsR-DBD using solution nuclear magnetic resonance (NMR) methods. The structure of ArsR-DBD consists of an N-terminal four-stranded beta-sheet, a helical core, and a C-terminal beta-hairpin. The overall tertiary fold of ArsR-DBD is most closely related to DBD structures of the OmpR/PhoB subfamily of bacterial RRs. To identify ArsR protein elements that potentially bind target DNA sequences and thereby regulate gene transcription in H. pylori, we modeled ArsR-DBD in complex with a putative DNA target. Additionally, we identified novel members of the ArsRS regulon by analyzing ArsR binding to the promoter sequences of putative target genes. These results broaden our understanding of the ArsRS TCS and its role in regulating gene expression in H. pylori.
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