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dc.creatorWeidner, Jason Lee
dc.date.accessioned2013-02-22T20:40:10Z
dc.date.available2013-02-22T20:40:10Z
dc.date.created2003
dc.date.issued2013-02-22
dc.identifier.urihttp://hdl.handle.net/1969.1/ETD-TAMU-2003-Fellows-Thesis-W325
dc.descriptionDue to the character of the original source materials and the nature of batch digitization, quality control issues may be present in this document. Please report any quality issues you encounter to digital@library.tamu.edu, referencing the URI of the item.en
dc.descriptionIncludes bibliographical references (leaves 26-27).en
dc.description.abstractAfter in vivo and in vitro experiments comparing wild type and S2 knockout strains of EIAV were conducted, the role of one small accessory protein still eluted discovery, S2. S2, is a small protein that has a nuclear localization sequence, SH3 binding domain ligand, and is only 19 kD in size. It was used in a bacterial two-hybrid to discover interacting host cell partner proteins from a mouse lung cDNA library via transcriptional activation. The experiment used a genetically modified strain of E. coli to test interactions between fusion products made by fusing S2 with lambda repressor, and random cellular proteins to RNA polymerase (RNAP). Since a reporter strain cassette is contained within the genetically altered bacteria, the lambda repressor can bind to the altered lambda operator, freeing the S2 particle for interaction. If a single bacteria has the plasmid that codes for S2 and the interacting partner, then the interacting partner can bind to S2, guiding RNAP to transcribe the reporter gene, carbenicillin. The experiment used plates with differing carbenicillin concentrations to test for stronger protein-protein interactions, and has resulted in about thirty different putative positive partners.en
dc.format.mediumelectronicen
dc.format.mimetypeapplication/pdf
dc.language.isoen_US
dc.publisherTexas A&M University
dc.rightsThis thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries in 2008. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use.en
dc.subjectbiochemistry.en
dc.subjectMajor biochemistry.en
dc.titleUsing the bacteria-2-hybrid system to determine the role of S2 in the equine infectious anemia virus (EIAV) life cycleen
thesis.degree.departmentbiochemistryen
thesis.degree.disciplinebiochemistryen
thesis.degree.nameFellows Thesisen
thesis.degree.levelUndergraduateen
dc.type.genrethesisen
dc.type.materialtexten
dc.format.digitalOriginreformatted digitalen


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