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| == Disease == | | == Disease == |
| There are mutations in H3.3 that are found in different types of bone tumors like [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4446520/ chrondroblastoma] for example and giant cell tumors of the bone. [https://cancerdiscovery.aacrjournals.org/content/3/12/1329.1 Chondroblastoma] arises in children and in young adults in the cartilage of the growth plates of the long bones and is most typically benign. | | There are mutations in H3.3 that are found in different types of bone tumors like [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4446520/ chrondroblastoma] for example and giant cell tumors of the bone. [https://cancerdiscovery.aacrjournals.org/content/3/12/1329.1 Chondroblastoma] arises in children and in young adults in the cartilage of the growth plates of the long bones and is most typically benign. |
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| == Relevance == | | == Relevance == |
Revision as of 23:58, 15 November 2020
Text To Be DisplayedHistone H3.3
| This is a default text for your page Sandbox GGC1. Click above on edit this page to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
histone H3 replaces H3 in a range of nucleosomes in active genes. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling
Disease
There are mutations in H3.3 that are found in different types of bone tumors like chrondroblastoma for example and giant cell tumors of the bone. Chondroblastoma arises in children and in young adults in the cartilage of the growth plates of the long bones and is most typically benign.
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 Lysine-36
Structural highlights
in a PubMed abstract,CENP-Awhich is a centromere-specific histone H3 variant is over expressed in cancer cells and it can be mislocalized ectopically in the form of heterotypic nucleosomes containing H3.3.
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- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:https://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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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).
2. Cancer Discovery Science Writers. Histone H3.3 Mutations Are Cancer Type-Specific. https://cancerdiscovery.aacrjournals.org/content/3/12/1329.1 (accessed Nov 14, 2020).
3. Kallappagoudar, S.; Yadav, R. K.; Lowe, B. R.; Partridge, J. F. Histone H3 mutations--a special role for H3.3 in tumorigenesis? https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4446520/ (accessed Nov 1, 2020).
4. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Histone H3.3. https://www.uniprot.org/uniprot/P84243 (accessed Nov 1, 2020).
