Examining the function of KIAA1310/NSL3, a member of the NSL, TET2 and TET3 epigenetic complexes
Khorasani, Abraham J.
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Eukaryotic 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]
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