Show simple item record

dc.contributor.authorKhorasani, Abraham J.en_US
dc.date.accessioned2015-08-04T20:28:19Z
dc.date.available2015-08-04T20:28:19Z
dc.date.issued2012en_US
dc.date.submitted2012en_US
dc.identifier.other(ALMA)contempen_US
dc.identifier.urihttps://hdl.handle.net/2144/12444
dc.descriptionThesis (M.A.)--Boston University PLEASE NOTE: Boston University Libraries did not receive an Authorization To Manage form for this thesis or dissertation. It is therefore not openly accessible, though it may be available by request. If you are the author or principal advisor of this work and would like to request open access for it, please contact us at open-help@bu.edu. Thank you.en_US
dc.description.abstractEukaryotic gene expression is regulated by a number of factors. Transcription initiation can be modulated by the binding of protein factors to specific sequences of DNA in the promoter of a gene. In addition, non-sequence (epigenetic) factors- namely, chemical modification of DNA and histones, the proteins around which DNA organizes to form chromatin - are a method of regulating gene expression by altering the structure of the chromatin environment and recruiting proteins that bind to the modifications. Two of the most common epigenetic modifications are acetylation of lysine residues on histones and methylation at the 5-position of the DNA base cytosine (5-methylcytosine, 5mC) within cytosine-guanine dinucleotides. Histone acetylation status is modulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs). DNA methylation is mediated by DNA methyltransferases (DNMTs); however, for some time, the mechanism of DNA demethylation was unclear. It was recently shown that the TET family of proteins was capable of oxidizing 5mC to 5-hydroxymethylcytosine (5hmC) and further on to 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) as part of a putative DNA demethylation pathway. Here, we have begun to study the largely uncharacterized protein KIAA1310/NSL3, which associates with MOF, a HAT, in the NSL complex, as well as TET2 and TET3. KIAA1310/NSL3 contains an a/β hydrolase fold domain, which we hypothesize to be important to its function in these epigenetic complexes. Little is known about its role in these complexes, although it has been shown to be involved in recruiting RNA polymerase II to the transcription start sites (TSSs) of genes regulated by the NSL complex. We aimed to investigate KIAA1310/NSL3's function in the context of the TET2 and TET3 complexes. [TRUNCATED]en_US
dc.language.isoen_USen_US
dc.publisherBoston Universityen_US
dc.titleExamining the function of KIAA1310/NSL3, a member of the NSL, TET2 and TET3 epigenetic complexesen_US
dc.typeThesis/Dissertationen_US
etd.degree.nameMaster of Artsen_US
etd.degree.levelmastersen_US
etd.degree.disciplineMedical Sciencesen_US
etd.degree.grantorBoston Universityen_US


This item appears in the following Collection(s)

Show simple item record