User:Madeleine Wilson/Sandbox 1: Difference between revisions
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=Lysine | =Histone Lysine Methyltransferase: Gene Activator= | ||
<StructureSection load='1O9S' size='350' frame='true' side='right' caption='Lysine Methyl Transferase' scene=’C_terminal_domain’> | <StructureSection load='1O9S' size='350' frame='true' side='right' caption='Lysine Methyl Transferase' scene=’C_terminal_domain’> | ||
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===Histone Methylation=== | ===Histone Methylation=== | ||
[[Image:human_nucleosome_ray_trace.png|200 px| right| thumb|Human nucleosome]] | [[Image:human_nucleosome_ray_trace.png|200 px| right| thumb|Human nucleosome, pbd code: 5y0c]] | ||
Histone proteins aid in the packing of DNA for the purpose of compacting the genome in the nucleus of the cell and regulating physical accessibility of genes for transcription. The protein itself is an octamer made of heterodimer core proteins H2a, H2b, H3, and H4, with H1 and H5 acting as linker proteins. About 145-157 base pairs wind around a histone core protein. <ref name="DesJarlais">PMID: 26745824</ref> Modifications to histone core proteins can affect the accessibility of genes in the genome and their ability to be transcribed. Some of these modifications include methylation/demethylation, acetylation/deacetylation, and ubiquitination/deubiquitination. <ref name="Lun">DOI: 10.1016/j.apsb.2013.04.007</ref> | Histone proteins aid in the packing of DNA for the purpose of compacting the genome in the nucleus of the cell and regulating physical accessibility of genes for transcription. The protein itself is an octamer made of heterodimer core proteins H2a, H2b, H3, and H4, with H1 and H5 acting as linker proteins. About 145-157 base pairs wind around a histone core protein. <ref name="DesJarlais">PMID: 26745824</ref> Modifications to histone core proteins can affect the accessibility of genes in the genome and their ability to be transcribed. Some of these modifications include methylation/demethylation, acetylation/deacetylation, and ubiquitination/deubiquitination. <ref name="Lun">DOI: 10.1016/j.apsb.2013.04.007</ref> | ||