Return to search

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

Indiana University-Purdue University Indianapolis (IUPUI) / The 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.

Identiferoai:union.ndltd.org:IUPUI/oai:scholarworks.iupui.edu:1805/28418
Date03 1900
CreatorsSegizbayeva, Lana
ContributorsGeorgiadis, Millie M., Mosley, Amber L., Wells, Clark D.
Source SetsIndiana University-Purdue University Indianapolis
Languageen_US
Detected LanguageEnglish
TypeThesis
RightsAttribution-NonCommercial-NoDerivatives 4.0 International, http://creativecommons.org/licenses/by-nc-nd/4.0/

Page generated in 0.0024 seconds