Project Advisor(s) (Students Only)
Dr. Lori Scott
Presentation Type (All Applicants)
Poster Presentation
Disciplines (All Applicants)
Bioinformatics | Biology | Genomics | Molecular Genetics
Description, Abstract, or Artist's Statement
Meiothermus ruber is a unique, red-pigmented, thermophilic bacterium that preferentially grows in high-temperature environments ranging from 35-70°C. Due to the lack of studies performed on this organism, there is quite a bit of information missing in regard to the genes found within this organism’s genome and their function. This study focuses in on the Mrub_1345 gene in M. ruber, which has been suggested to be orthologous to the proC gene found of E. coli proline biosynthesis pathway. To test if these genes are orthologs, we performed the complementation assay on wild-type proC. Next, we performed site-directed mutagenesis on amino acids that are suspected to play an important role in enzyme functionality, and then repeated the complementation assay. A missense mutation swapping a glycine residue to aspartate was shown to have no effect on M. ruber proC functionality. We are currently working on preparing more mutant versions of this gene for further studies.
Augustana Digital Commons Citation
Wills, Brandon M. and Scott, Lori R.. "Effects of mutating the Mrub_1345 gene found in Meiothermus Ruber" (2016). Celebration of Learning.
https://digitalcommons.augustana.edu/celebrationoflearning/2016/posters/4
Effects of mutating the Mrub_1345 gene found in Meiothermus Ruber
Meiothermus ruber is a unique, red-pigmented, thermophilic bacterium that preferentially grows in high-temperature environments ranging from 35-70°C. Due to the lack of studies performed on this organism, there is quite a bit of information missing in regard to the genes found within this organism’s genome and their function. This study focuses in on the Mrub_1345 gene in M. ruber, which has been suggested to be orthologous to the proC gene found of E. coli proline biosynthesis pathway. To test if these genes are orthologs, we performed the complementation assay on wild-type proC. Next, we performed site-directed mutagenesis on amino acids that are suspected to play an important role in enzyme functionality, and then repeated the complementation assay. A missense mutation swapping a glycine residue to aspartate was shown to have no effect on M. ruber proC functionality. We are currently working on preparing more mutant versions of this gene for further studies.