4.5 Article

Unraveling the histone's potential A proteomics perspective

Journal

EPIGENETICS
Volume 3, Issue 5, Pages 254-257

Publisher

TAYLOR & FRANCIS INC
DOI: 10.4161/epi.3.5.7005

Keywords

histone; post-translational modification; proteomics; mass spectrometry; epigenetics

Funding

  1. NHGRI NIH HHS [T32 HG002760-06, T32 HG002760-05, T32 HG002760] Funding Source: Medline
  2. 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

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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.

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