H3K36me
 | This article contains close paraphrasing of a non-free copyrighted source, https://tools.wmflabs.org/copyvios/?lang=en&project=wikipedia&title=H3K36me&oldid=&action=search&use_engine=1&use_links=1&turnitin=0 (Copyvios report). (September 2018) |
H3K36me (Histone H3 lysine 36 methylation) is a histone modification involved in epigenetic regulation and is a common epigenetic mark.[1] The modifications of H3K36 are very diverse and play roles in many important biological processes such as DNA replication, transcription, recombination and repair of DNA damage.[2] The misregulation of H3K36 methyltransferases is connected with a number of human diseases, underscoring the importance of this modification.[3]
Modification
The main role in the alteration of chromatine structure plays post-translational modification and these modification dictate epigenetic inheritance. The state of chromatine define three groups of protein: proteins which add modifications to specific histone residues, proteins which recognize modifications and recruits effector and proteins which removes unnecessary modifications. These three group of proteins co-operate in many cellular processes like: cell proliferation, differentiation, and environmental adaptation and it is important to maintain cellular homeostasis.[1]
H3K36me comprises three states: mono-, di-, and tri-methylation of lysine side chain amino groups and these states have different distribution and function. There is a shift from mono, to di, to tri methylation from the promoter to the 3’ end active genes.[4] For the addition of methyl groups to specific histone Lys or Arg residues, histone methyltransferase (HMTase) enzymes use S-adenosyl methionine.[5] All of the H3K36-specific methyltransferases identified thus far have the catalytic SET domain in common, but they have varying preferences for Lys36 residues in different methylation states. The main function of SET2 is modification of histone H3K36 via katalitic SET domain.
H3K36me and human diseases
Methylation of H3K36 regulates diverse cellular processes and defective regulation of H3K36me leads to number of human diseases.[5] Some of the recently identified oncogenic histone mutations are at or close to H3K36 and are associated with diseases such as chondroblastomas and gliomas.[3] Defects in the genes that maintain the levels of H3K36 methylation cause developmental defects and disease. Defects in SETD2 leads to sporadic clear renal cell carcinoma and also it can be a tumor suppressor in breast cancer. Defects in each member of the NSD (nuclear receptor SET domain-containing) family have been implicated in multiple diseases and cancer types. For example, in lung and prostate cancer, acute myeloid leukemia (AML) and refractory anemia.[5]
References
- ^ a b Suzuki S, Murakami Y, Takahata S (January 2017). "H3K36 methylation state and associated silencing mechanisms". Transcription. 8 (1): 26–31. doi:10.1080/21541264.2016.1246076. PMC 5279713. PMID 27723431.
- ^ Lee JS, Smith E, Shilatifard A (September 2010). "The language of histone crosstalk". Cell. 142 (5): 682–5. doi:10.1016/j.cell.2010.08.011. PMC 3711869. PMID 20813257.
- ^ a b Zhang Y, Shan CM, Wang J, Bao K, Tong L, Jia S (March 2017). "Molecular basis for the role of oncogenic histone mutations in modulating H3K36 methylation". Scientific Reports. 7 (1): 43906. Bibcode:2017NatSR...743906Z. doi:10.1038/srep43906. PMC 5335568. PMID 28256625.
- ^ Barski A, Cuddapah S, Cui K, Roh TY, Schones DE, Wang Z, Wei G, Chepelev I, Zhao K (May 2007). "High-resolution profiling of histone methylations in the human genome". Cell. 129 (4): 823–37. doi:10.1016/j.cell.2007.05.009. PMID 17512414.
- ^ a b c Wagner EJ, Carpenter PB (January 2012). "Understanding the language of Lys36 methylation at histone H3". Nature Reviews. Molecular Cell Biology. 13 (2): 115–26. doi:10.1038/nrm3274. PMC 3969746. PMID 22266761.