CHD4 Sandbox: Difference between revisions

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The NuRD complex is comprised of histone protein deacetylase 1/2 HDAC1/HDAC2, GATA2A ,GATA2b, MTA1 ,MTA2, MTA3, MBD2, MBD3, RBBP7, RBBP4, and CHD3, CHD4, CHD5[3]. HDAC1/2 is responsible for the deacetylation of lysine residues on the histone tails, Gata2a/2b are zinc fingers that bind DNA and scaffold to Mbd2/3 which is a Methyl CpG domain that interacts methylated DNA[3]. Rbbp4/7 acts as a scaffold for MTA1 and bind to Histone H4, while MTA1 has a GATA and HDAC binding domain connecting the NuRD complex[3].  
The NuRD complex is comprised of histone protein deacetylase 1/2 HDAC1/HDAC2, GATA2A ,GATA2b, MTA1 ,MTA2, MTA3, MBD2, MBD3, RBBP7, RBBP4, and CHD3, CHD4, CHD5[3]. HDAC1/2 is responsible for the deacetylation of lysine residues on the histone tails, Gata2a/2b are zinc fingers that bind DNA and scaffold to Mbd2/3 which is a Methyl CpG domain that interacts methylated DNA[3]. Rbbp4/7 acts as a scaffold for MTA1 and bind to Histone H4, while MTA1 has a GATA and HDAC binding domain connecting the NuRD complex[3].  
==The Nucleosome==
==The Nucleosome==
The nucleosome is comprised of 146-147 DNA base pairs <scene name='88/880268/147-mer/2'>146-147 DNA base pairs</scene> wrapped around an octamer of four different proteins called histones.  
The nucleosome is comprised of <scene name='88/880268/147-mer/2'>146-147 DNA base pairs</scene> wrapped around an <scene name='88/880268/147-mer_octamer/1'>octamer</scene> of four different proteins called histones.  
===The Histones===
===The Histones===
The four histone proteins: H4, H3, H2A, and H2B make up the nucleosome with two sets of two heterodimers[2]. Heterodimers consisting of H3 and H4 as well as H2A and H2B[2]. These heterodimers form an octamer through the presence of hydrophobic interaction between dimers[2].
The four histone proteins: H4, H3, H2A, and H2B make up the nucleosome with two sets of two heterodimers[2]. Heterodimers consisting of H3 and H4 as well as H2A and H2B[2]. These heterodimers form an octamer through the presence of hydrophobic interaction between dimers[2].
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