Date of Award

Spring 2015

Document Type

Thesis

Terms of Use

© 2015 Jason Hua. All rights reserved. This work is freely available courtesy of the author. It may only be used for non-commercial, educational, and research purposes. For all other uses, including reproduction and distribution, please contact the copyright holder.

Degree Name

Bachelor of Arts

Department

Chemistry & Biochemistry Department

First Advisor

Stephen T. Miller

Abstract

A diverse range of Gram-negative and Gram-positive bacteria rely on density-dependent, intercellular communication mediated by small signaling molecules called auto inducers to coordinate synchronous gene expression through a process termed quorum sensing. One family of auto inducers, consisting of spontaneously interconverting derivatives of (4S)-4,S-dihydroxy-2,3-pentanedione (DPD) and collectively referred to as Autoinducer- 2 (AI-2), is recognized in a wide variety of species by one of two canonical receptor proteins: LuxP, exclusive to the genus Vibrio, or an LsrB-like receptor. However, several studies have reported that two predicted ribose-binding proteins (RbsB), from Haemophilus injluenzae and Aggregatibacter actinomycetemcomitans, might behave as functional AI-2 receptors. In this study, I perform a series of bioinformatics studies to assess the similarity of these RbsB proteins to LsrB and LuxP and attempt to probe their ability to bind AI-2 through structural data and a Vibrio harveyi reporter bioassay. I also present the expression and purification of an N-terminal deleted construct of LsrR (C-LsrR), the transcriptional repressor of the lsr operon, for use in future in vitro binding assays and crystallographic studies.

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