DOI
https://doi.org/10.25772/EAG1-5612
Author ORCID Identifier
0000-0002-2491-3627
Defense Date
2017
Document Type
Thesis
Degree Name
Master of Science
Department
Microbiology & Immunology
First Advisor
Peter Uetz
Abstract
With the number of fully sequenced bacterial genomes increasing in the past 7 years, it has been discovered that a large percentage of the putative protein coding genes have no known function. This lack of knowledge leaves scientists with an incomplete understanding of bacteria. In this study, conserved hypothetical protein mutants from Streptococcus sanguinis SK36 were screened on solid media with various environmental conditions. From these screens, the candidate protein, SSA_2372, displayed a sensitivity to acidic conditions. Its homolog in Bacillus subtilis 168, BSU00030, also displayed a sensitivity to pH conditions at its acid tolerance extremes unlike its other homolog in Escherichia coli, YbcJ. When the growth rate and cell yield was acquired, the sensitivity was shown to be significant for both SSA_2372 and BSU00030 mutants. Through data mining, it was determined that Firmicutes in this homolog family COG2501 may function as a regulator for recombination protein F.
Rights
© The Author
Is Part Of
VCU University Archives
Is Part Of
VCU Theses and Dissertations
Date of Submission
5-17-2017