Graduation Year
2017
Graduation Month
May
Document Type
Professional Paper - Campus Access Only
Degree Name
Bachelor of Science
School or Department
Chemistry and Biochemistry, Department of
Major
Biochemistry
Faculty Mentor Department
Biological Sciences, Division of
Faculty Mentor
Dr. Scott Samuels
Faculty Reader(s)
Dr. Scott Samuels
Keywords
Borrelia burgdorferi, rpoS transcript, RNase Y, cleavage assay, protein purification
Subject Categories
Biochemistry | Molecular Biology
Abstract
Borrelia burgdorferi is the bacterial agent that causes Lyme disease. The pathogenic bacteria are transmitted to vertebrates through tick feeding and are maintained in nature in an enzootic cycle. The expression of outer surface protein OspC is essential for B. burgdorferi to move from the tick to a mammal. Alternative sigma factor RpoS is responsible for inducing gene (ospC) expression for OspC production during the enzootic cycle. Two versions of rpoS transcripts are observed in vivo: a long one, which is hypothesized to be required for transmission from the tick, and a short one, which is thought to be involved in infection of the mammal. The goal of this project is to understand the mechanism of how the long rpoS transcript is processed so that RpoS protein can activate ospC expression during transmission. We hypothesize that the long rpoS transcript is cleaved by ribonuclease (RNase) Y at the 5′ end. Two specific aims were conducted during the research project: (1) In vitro cleavage assays using purified recombinant RNase Y and artificial rpoS mRNA substrates and (2) constructing a strain of B. burgdorferi that expresses a recombinant RNase Y with a 10X-histidine tag in order to directly purify RNase Y.
Honors College Research Project
1
Recommended Citation
Zhou, Zhibing, "The Role of RNase Y in rpoS Transcript Processing in Borrelia burgdorferi" (2017). Undergraduate Theses, Professional Papers, and Capstone Artifacts. 72.
https://scholarworks.umt.edu/utpp/72
© Copyright 2017 Zhibing Zhou