The phosphorylation of the RNA polymerase II C-terminal domain (CTD) plays a key role in delineating transcribed regions within chromatin by recruiting histone methylases and deacetylases.
Using genome-wide nucleosome mapping, we show that CTD S2 phosphorylation controls nucleosome dynamics in the promoter of a subset of 324 genes, including the regulators of cell differentiation .
Most genes were expressed as normal in these yeast cells, but a few hundred genes were not expressed. then used a technique called MNase-Seq to map the position of nucleosomes across the genome and found that there were more nucleosomes near to start of these down-regulated genes.
- Free sign up malaysian adult live cam
- Sex free sex chat
- best absolutely online dating sites
- the independent dating
- firemandatingsite com
- dr samantha cole s online dating manual for women
Available data support that these domains are responsible for the H3 methylation-dependent recruitment of HDACs.
For example, the chromodomain protein Eaf3 is a subunit of Rpd3C(S) deacetylase and binds H3K36me (Carrozza et al., 2005; Keogh et al., 2005).
RNA polymerase II is the enzyme that carries out transcription of messenger RNAs in all eukaryotic cells—that is, the cells of organisms like plants, animals, and fungi.
Like all enzymes, RNA polymerase II is made of smaller building blocks called amino acids.
The distribution of histone H3K4 and K36 methylation mirrors CTD phosphorylation due to the direct recruitment of the H3 methyltransferases Set1-COMPASS (for H3K4) and Set2 (for H3K36) by the S5P and S2P of Pol II, respectively (Ng et al., 2003; Keogh et al., 2005).
Set1 is the only H3K4 methyltransferase in yeast, but it produces monomethylation, dimethylation, and trimethylation states.One end of the RNA polymerase II enzyme, called the C-terminal domain (or CTD), contains a unique sequence of amino acids that serves as a scaffold to recruit other proteins involved in transcription and histone modifications.Different amino acids in this region of RNA polymerase II can be modified by the addition of phosphate groups.However, most of the DNA in a cell is wrapped around proteins called histones to make structures known as nucleosomes, and the DNA has to be unpacked to allow the enzymes that make messenger RNA to access it.Cells regulate how the DNA is packed by attaching chemical groups to the histone proteins.Set2 targets H3K36me2 and me3 that are both highest near the 3′-end (Krogan et al., 2003; Kizer et al., 2005).