Title

The role of RNase Y in rpoS transcript processing in B. burgdorferi

Presentation Type

Presentation

Abstract

Lyme disease affects an estimated 300,000 Americans yearly, and, if untreated, can be deadly. Borrelia burgdorferi, the bacterium that causes Lyme disease, is likely transmitted to hosts in a process involving rpoS messenger RNA (mRNA) processing via ribonucleases (RNases). RNases are enzymes that degrade the nucleic acid RNA and are involved in many molecular processes in cells. B. burgdorferi requires a change in gene expression to transmit from its tick vector to a mammalian host. Transmission depends on a complicated cascade of regulatory factors, including the alternative sigma factor, RpoS. Sigma factors are a component of RNA polymerase, the enzyme that transcribes genes. RpoS production requires the translation of a processed rpoS mRNA; however, the mechanism by which this rpoS mRNA is processed is unknown. I am investigating whether the rpoS mRNA is cleaved by RNase Y in B. burgdorferi. Previous research in Bacillus subtilis shows that this enzyme appears to be responsible for both global mRNA stability and degradation. To this end, I am attempting to obtain RNase Y by overexpression of recombinant RNase Y with a truncated transmembrane domain and subsequent purification using the IMPACT system. I am using this purified protein to characterize the potential processing site of the rpoS mRNA by using various artificial rpoS mRNA substrates through an in vitro cleavage assay. This research will contribute to a better understanding of the transmission mechanism of B. burgdorferi and of the function of RNase Y. Additionally, this project has the potential to provide the basis for developing new antimicrobial therapies against Lyme disease. If identified as crucial to transmission of Lyme disease to hosts, the thorough characterization of RNase Y activity in processing mRNA will reveal specific targets for drug and therapy development.

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Life Sciences

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Apr 11th, 4:20 PM Apr 11th, 4:40 PM

The role of RNase Y in rpoS transcript processing in B. burgdorferi

Lyme disease affects an estimated 300,000 Americans yearly, and, if untreated, can be deadly. Borrelia burgdorferi, the bacterium that causes Lyme disease, is likely transmitted to hosts in a process involving rpoS messenger RNA (mRNA) processing via ribonucleases (RNases). RNases are enzymes that degrade the nucleic acid RNA and are involved in many molecular processes in cells. B. burgdorferi requires a change in gene expression to transmit from its tick vector to a mammalian host. Transmission depends on a complicated cascade of regulatory factors, including the alternative sigma factor, RpoS. Sigma factors are a component of RNA polymerase, the enzyme that transcribes genes. RpoS production requires the translation of a processed rpoS mRNA; however, the mechanism by which this rpoS mRNA is processed is unknown. I am investigating whether the rpoS mRNA is cleaved by RNase Y in B. burgdorferi. Previous research in Bacillus subtilis shows that this enzyme appears to be responsible for both global mRNA stability and degradation. To this end, I am attempting to obtain RNase Y by overexpression of recombinant RNase Y with a truncated transmembrane domain and subsequent purification using the IMPACT system. I am using this purified protein to characterize the potential processing site of the rpoS mRNA by using various artificial rpoS mRNA substrates through an in vitro cleavage assay. This research will contribute to a better understanding of the transmission mechanism of B. burgdorferi and of the function of RNase Y. Additionally, this project has the potential to provide the basis for developing new antimicrobial therapies against Lyme disease. If identified as crucial to transmission of Lyme disease to hosts, the thorough characterization of RNase Y activity in processing mRNA will reveal specific targets for drug and therapy development.