- Name: Julia E. Martin, Ph.D.
- Institution: Idaho State University
- Department: Biological Sciences
- Phone: 208-282-1277
- Email: email@example.com
Summary: We are interested in how bacteria sense, respond, and adapt to metal ion changes in their surrounding environment. More specifically, we study the physiological underpinnings and molecular mechanisms of how cells regulate transition metal ion homeostasis and manganese detoxification in the model Gram-positive bacterium and respiratory pathogen Streptococcus pneumoniae.
Manganese is an essential trace nutrient that serves as a required cofactor in bacteria, and is largely recognized for its role in oxidative stress resistance and in enhancing virulence of bacterial pathogens. However, when in excess, manganese can impair bacterial growth, the mechanism of which is poorly explored. Thus far, we have shown that excess manganese causes an imbalance in intracellular transition metal ion pools, which potentially affects enzyme activity. Current studies seek to (i) further our understanding of the regulation and trafficking of intracellular manganese and (ii) identify enzyme targets that are disrupted during manganese-stress in S. pneumoniae.
Minimum classes: General Biology, General Chemistry, Microbiology, Biochemistry
Projects: We use a variety of techniques and approaches that span the interface of biology and chemistry to study manganese homeostasis and detoxification. Classical microbiology and molecular biology techniques include microbial culture, microscopy, genetic manipulations, site-directed mutagenesis, molecular cloning, and quantitative real-time PCR. Biochemistry techniques include protein expression and purification, enzyme assays, protein interactions, western blot, and structure modeling.
Possible project areas include:
1) Investigating the regulation of the manganese efflux pump, MntE, in S. pneumoniae.
2) Investigating the impact of manganese toxicity on other transition metal ion pools.
3) Investigating the effect of metal availability on enzyme activity.