Generating an expression construct and soluble protein for characterization studies of a putative RNA m5C methyltransferase, yeast ORF YNLO22c

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dc.contributor.advisor Redman, Kent L en_US
dc.contributor.author Craft, Jennifer Leigh en_US
dc.date.accessioned 2011-06-03T19:40:33Z
dc.date.available 2011-06-03T19:40:33Z
dc.date.created 2005 en_US
dc.date.issued 2005
dc.identifier LD2489.Z78 2005 .C73 en_US
dc.identifier.uri http://cardinalscholar.bsu.edu/handle/handle/187948
dc.description.abstract RNA m5C methyltransferases are a group of enzymes that catalyze the transfer of a methyl group to a cytosine nucleotide of RNA. Only two of these enzymes have been well characterized: Fmu from E. coli and Trm4p from S. cerevisiae. YNLO22c is one of three ORFs identified in S. cerevisiae that have homology with both known and putative RNA m5C methyltransferases, but its encoded protein, YNLO22p, has not been confirmed to have enzyme activity. Verifying that YNLO22c encodes an RNA m5C methyltransferase will require adequate amounts of soluble YNLO22p for enzyme assays. A bacterial expression plasmid for YNLO22c was developed, but the result was insoluble protein. Therefore, several methods known to improve protein solubility were tested to develop a system in which a sufficient amount of soluble YNLO22p could be produced. Results of this study found that coexpression of YNLO22c with chaperone proteins can provide sufficient quantities of soluble YNLO22p.
dc.description.sponsorship Department of Biology
dc.format.extent vii, 71 leaves : ill. (some col.) ; 28 cm. en_US
dc.source Virtual Press en_US
dc.subject.lcsh Recombinant proteins -- Solubility. en_US
dc.subject.lcsh Transfer RNA. en_US
dc.subject.lcsh Methyltransferases. en_US
dc.title Generating an expression construct and soluble protein for characterization studies of a putative RNA m5C methyltransferase, yeast ORF YNLO22c en_US
dc.description.degree Thesis (M.S.)
dc.identifier.cardcat-url http://liblink.bsu.edu/catkey/1319220 en_US


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  • Master's Theses [5318]
    Master's theses submitted to the Graduate School by Ball State University master's degree candidates in partial fulfillment of degree requirements.

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