Investigation of Protein – Protein Interactors of Setmar Using Tandem Mass Tag Mass Spectrometry

dc.contributor.advisorGeorgiadis, Millie M.
dc.contributor.authorSegizbayeva, Lana
dc.contributor.otherMosley, Amber L.
dc.contributor.otherWells, Clark D.
dc.date.accessioned2022-04-06T18:17:27Z
dc.date.available2022-04-06T18:17:27Z
dc.date.issued2022-03
dc.degree.date2022en_US
dc.degree.disciplineDepartment of Biochemistry & Molecular Biologyen
dc.degree.grantorIndiana Universityen_US
dc.degree.levelM.S.en_US
dc.descriptionIndiana University-Purdue University Indianapolis (IUPUI)en_US
dc.description.abstractThe nuclear protein SETMAR has been reported to be involved in many processes such as non-homologous end joining (NHEJ), di-methylation (arguably) of K36 of histone H3, restart of stalled replication forks, chromosome decatenation, enhancing of TOPII inhibitors which results in resistance to chemotherapeutics in cancer patients, etc. All these purported functions are impossible to execute without interaction with other proteins. It is established that SETMAR binds specifically to DNA at terminal inverted repeat sequences and can loop DNA. This DNA sequence specific pull-down exploits this attribute to identify possible protein interactors of SETMAR. As a result of this experiment several proteins have been identified for further research: BAG2, c12orf45, PPIA, XRCC5/6, and ZBTB43, all of which are found in higher statistical abundances in full length SETMAR samples.en_US
dc.identifier.urihttps://hdl.handle.net/1805/28418
dc.identifier.urihttp://dx.doi.org/10.7912/C2/2887
dc.language.isoen_USen_US
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectSETMARen_US
dc.subjectmass spectrometryen_US
dc.subjectlysine methyltransferaseen_US
dc.subjectbiotinen_US
dc.subjectMetnaseen_US
dc.subjectstreptavidinen_US
dc.titleInvestigation of Protein – Protein Interactors of Setmar Using Tandem Mass Tag Mass Spectrometryen_US
dc.typeThesisen
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