Journal
EPIGENETICS
Volume 3, Issue 5, Pages 254-257Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/epi.3.5.7005
Keywords
histone; post-translational modification; proteomics; mass spectrometry; epigenetics
Funding
- NHGRI NIH HHS [T32 HG002760-06, T32 HG002760-05, T32 HG002760] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008349, R01 GM080148, T32 GM008349-18, T32 GM008349-19, P01 GM081629, T32 GM008349-15, T32 GM008349-15S1, T32 GM008349-20, T32 GM008349-10, T32 GM008349-17, T32 GM008349-16, T32 GM008349-13, T32 GM008349-11, T32 GM008349-12, P01 GM081629-01A10001, T32 GM008349-14, R01 GM080148-02] Funding Source: Medline
Ask authors/readers for more resources
Post translational modification (PTM) of histones has long been associated with epigenetic regulation. Although genomic approaches have established correlation between a handful of histone PTMs and transcriptional states, only recently have advancements in proteomics provided the tools necessary to study histone proteins and their relevant modifications in this context. Using mass spectrometry, researchers have demonstrated the ability to determine the full repertoire of histone PTMs, their residue specific location, the combinations in which they exist, and the proteins that interact with these combinations. Moving forward it will be imperative to develop novel approaches that combine proteomic and genomic technologies to determine the functional significance of these combinations of modifications. Assays with increased specificity will resolve more focused biological questions and determine to what extent, and by what mechanisms, histones influence transcription.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available