Publications by authors named "Rebecca K Phillips"

Article Synopsis
  • - The study reveals that the MtrR protein, which normally represses the expression of the multidrug efflux pump (MtrCDE), is induced in the presence of certain bile salts, allowing the bacteria to expel harmful compounds, enhancing its survival against host-derived antimicrobials.
  • - Researchers determined the crystal structure of MtrR, identifying a binding pocket that hints at how bile salts could serve as natural inducers, specifically highlighting interactions with chenodeoxycholate and taurodeoxycholate.
  • - The findings shed light on how the pathogen, responsible for gonorrheal infections and its rising antibiotic resistance, utilizes bile salts to bypass human immune defenses, suggesting potential new avenues for combating resistant bacterial strains.
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Kinesin-1, -2, -5, and -7 generate processive hand-over-hand 8-nm steps to transport intracellular cargoes toward the microtubule plus end. This processive motility requires gating mechanisms to coordinate the mechanochemical cycles of the two motor heads to sustain the processive run. A key structural element believed to regulate the degree of processivity is the neck-linker, a short peptide of 12-18 residues, which connects the motor domain to its coiled-coil stalk.

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Unusual deoxy sugars are often attached to natural products such as antibiotics, antifungals, and chemotherapeutic agents. One such sugar is mycinose, which has been found on the antibiotics chalcomycin and tylosin. An intermediate in the biosynthesis of mycinose is dTDP-6-deoxy-D-allose.

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The streptococcal coaggregation regulator (ScaR) of Streptococcus gordonii is a manganese-dependent transcriptional regulator. When intracellular manganese concentrations become elevated, ScaR represses transcription of the scaCBA operon, which encodes a manganese uptake transporter. A member of the DtxR/MntR family of metalloregulators, ScaR shares sequence similarity with other family members, and many metal-binding residues are conserved.

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