Sandbox GGC1: Difference between revisions
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'''Histone H3.3'''<StructureSection load='3WTP' size='340' side='right' caption='Caption for this structure' scene=''> | '''Histone H3.3'''<StructureSection load='3WTP' size='340' side='right' caption='Caption for this structure' scene=''> | ||
== Introduction == | == Introduction == | ||
Histone H3.3 is a variant histone of H3 which has the gene name H3.3A and this particular protein is found in Humans. the location of this can be found in the nucleus and in the chromosome. | Histone H3.3 is a variant histone of H3 which has the gene name H3.3A and this particular protein is found in Humans. the location of this can be found in the nucleus and in the chromosome.<ref>https://www.uniprot.org/uniprot/P84243</ref> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/P84243 Histone H3] replaces H3 in a range of nucleosomes in active genes and it takes over the original H3 in non dividing cells. Nucleosomes wrap around and compact DNA into chromatin which limits DNA access to cellular machineries which need DNA as a template. Histones play an important role in regulation of transcription, DNA repair, DNA replication and also chromosomal stability. Access to DNA is regulated by post-translational modifications of histones which is called a histone code, and nucleosome remodeling. It also serves as a replacement histone that's imbedded chromatin regions by the HIRA chaperone, after the depletion of the H3.1 during transcription and DNA repair. | [https://www.uniprot.org/uniprot/P84243 Histone H3] replaces H3 in a range of nucleosomes in active genes and it takes over the original H3 in non dividing cells. Nucleosomes wrap around and compact DNA into chromatin which limits DNA access to cellular machineries which need DNA as a template. Histones play an important role in regulation of transcription, DNA repair, DNA replication and also chromosomal stability. Access to DNA is regulated by post-translational modifications of histones which is called a histone code, and nucleosome remodeling. It also serves as a replacement histone that's imbedded chromatin regions by the HIRA chaperone, after the depletion of the H3.1 during transcription and DNA repair.<ref>https://www.uniprot.org/uniprot/P84243</ref> | ||
== Disease == | == Disease == | ||
There have been studies that have identified mutations encoding a K27M substitution and there have also been mutations that encoded | There have been studies that have identified mutations encoding a K27M substitution and there have also been mutations that encoded | ||
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== Relevance == | == Relevance == | ||
Histone octamer containing two of H2A, H2B, H3 and H4 and the octamer wraps 147bp of DNA. H3.3 interacts with HIRA which is a chaperone and ZMYND11 when trimethylated at <scene name='75/752263/3wtp/2'>Lysine-36</scene> (color coded dark blue). HIRA can deposit histones of H3.3 in replicating and non replicating cells. Also in the HIRA complex, Anti slicing factors ASF1a and ASF1b are purified by H3.3. However, when there's a disappearance of HIRA which is responsible for H3.3 deposition, it can cause defects in the early stages of embryogenesis. ZMYND11 also known as BS69 can find H3.3 LYS 36 (H3.3K36me3) by the binding domain of chromatin. | Histone octamer containing two of H2A, H2B, H3 and H4 and the octamer wraps 147bp of DNA. H3.3 interacts with HIRA which is a chaperone and ZMYND11 when trimethylated at <scene name='75/752263/3wtp/2'>Lysine-36</scene> (color coded dark blue). HIRA can deposit histones of H3.3 in replicating and non replicating cells. Also in the HIRA complex, Anti slicing factors ASF1a and ASF1b are purified by H3.3. However, when there's a disappearance of HIRA which is responsible for H3.3 deposition, it can cause defects in the early stages of embryogenesis. ZMYND11 also known as BS69 can find H3.3 LYS 36 (H3.3K36me3) by the binding domain of chromatin. | ||
== Structural highlights == | == Structural highlights == | ||
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references /> | |||
1. Arimura, Y.; Shirayama, K.; Horikoshi, N.; Fujita, R.; Taguchi, H.; Kagawa, W.; Fukagawa, T.; Almouzni, G.; Kurumizaka, H. Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3. https://www.nature.com/articles/srep07115 (accessed Nov 1, 2020). | 1. Arimura, Y.; Shirayama, K.; Horikoshi, N.; Fujita, R.; Taguchi, H.; Kagawa, W.; Fukagawa, T.; Almouzni, G.; Kurumizaka, H. Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3. https://www.nature.com/articles/srep07115 (accessed Nov 1, 2020). | ||