Presentation Title: Investigating a SloR Q170A mutation on SloR:SRE binding in Streptococcus mutans

Section: Poster Session Group 2 2

Location: , Great Hall

Date & Time: Friday, April 19, 2013 - 2:45pm - 3:30pm


Streptococcus mutans is the primary causative agent of dental caries in humans.   The SloR protein is of interest to the Spatafora laboratory where it has been shown to bind recognition elements (SREs) at or near promoter regions in a manganese-dependent manner. As a metalloregulatory protein, the ability of SloR to regulate downstream genes depends on its ability to bind metal ions at each of two sites within its predicted dimerization domain.  We propose that a glutamine (Q) at position 170 within the SloR FeoA domain may be important for coordinating metal ion binding at site 1.  This is true of SloR homologues in Corynebacterium diphtheria (DxtR) and Mycobacterium tuberculosis (IdeR).  The present study investigates the impact of a Q170A mutation on SloR:SRE binding in electrophoretic mobility shift assays. Preliminary results are consistent with a unique mechanism for metal ion binding at site 1.  This research can reveal potential targets for the development of an anti-caries therapeutic. 

Type of Presentation: Individual poster

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Presentation Topic: NA

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Format: Poster Session

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Presenter Information
Presenter(s): Benz, Karl Statesir
Major(s): Molecular Biology and Biochemistry
Class Year(s): 2013

Sponsor(s): Spatafora, Grace A.
Dept(s): Molecular Biology and Biochemistry

Moderator: ,