Interactions of the Metalloregulatory Protein SloR from Streptococcus mutans with Its Metal Ion Effectors and DNA Binding Site

Journal of Bacteriology
G A SpataforaArthur Glasfeld

Abstract

Streptococcus mutans is the causative agent of dental caries, a significant concern for human health, and therefore an attractive target for therapeutics development. Previous work in our laboratory has identified a homodimeric, manganese-dependent repressor protein, SloR, as an important regulator of cariogenesis and has used site-directed mutagenesis to map functions to specific regions of the protein. Here we extend those studies to better understand the structural interaction between SloR and its operator and its effector metal ions. The results of DNase I assays indicate that SloR protects a 42-bp region of DNA that overlaps the sloABC promoter on the S. mutans UA159 chromosome, while electrophoretic mobility shift and solution binding assays indicate that each of two SloR dimers binds to this region. Real-time semiquantitative reverse transcriptase PCR (real-time semi-qRT-PCR) experiments were used to determine the individual base pairs that contribute to SloR-DNA binding specificity. Solution studies indicate that Mn(2+) is better than Zn(2+) at specifically activating SloR to bind DNA, and yet the 2.8-Å resolved crystal structure of SloR bound to Zn(2+) provides insight into the means by which selective activation by Mn...Continue Reading

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Citations

Nov 5, 2016·Molecular Oral Microbiology·S C CreppsG A Spatafora
Dec 21, 2019·The Journal of Biological Chemistry·Karina A Baksh, Deborah B Zamble
Mar 20, 2020·Molecular Microbiology·Tridib GangulyJosé A Lemos
Jan 25, 2021·The Journal of Biological Chemistry·Karina A Baksh, Deborah B Zamble

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