Identification and Interrogation of Combinatorial Histone Modifications
Histone proteins are dynamically modified to mediate a variety of cellular processes including gene transcription, DNA damage repair, and apoptosis. Regulation of these processes occurs through the recruitment of non-histone proteins to chromatin by specific combinations of histone post-translation...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2013-12-01
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| Series: | Frontiers in Genetics |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fgene.2013.00264/full |
| _version_ | 1828190766050050048 |
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| author | Kelly R Karch Jamie E DeNizio Ben E Black Benjamin Aaron Garcia |
| author_facet | Kelly R Karch Jamie E DeNizio Ben E Black Benjamin Aaron Garcia |
| author_sort | Kelly R Karch |
| collection | DOAJ |
| description | Histone proteins are dynamically modified to mediate a variety of cellular processes including gene transcription, DNA damage repair, and apoptosis. Regulation of these processes occurs through the recruitment of non-histone proteins to chromatin by specific combinations of histone post-translational modifications (PTMs). Mass spectrometry has emerged as an essential tool to discover and quantify histone PTMs both within and between samples in an unbiased manner. Developments in mass spectrometry that allow for characterization of large histone peptides or intact protein has made it possible to determine which modifications occur simultaneously on a single histone polypeptide. A variety of techniques from biochemistry, biophysics, and chemical biology have been employed to determine the biological relevance of discovered combinatorial codes. This review first describes advancements in the field of mass spectrometry that have facilitated histone PTM analysis and then covers notable approaches to probe the biological relevance of these modifications in their nucleosomal context. |
| first_indexed | 2024-04-12T08:28:18Z |
| format | Article |
| id | doaj.art-0c248f412f414f52a745ad2e66ec6d35 |
| institution | Directory Open Access Journal |
| issn | 1664-8021 |
| language | English |
| last_indexed | 2024-04-12T08:28:18Z |
| publishDate | 2013-12-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Genetics |
| spelling | doaj.art-0c248f412f414f52a745ad2e66ec6d352022-12-22T03:40:18ZengFrontiers Media S.A.Frontiers in Genetics1664-80212013-12-01410.3389/fgene.2013.0026469905Identification and Interrogation of Combinatorial Histone ModificationsKelly R Karch0Jamie E DeNizio1Ben E Black2Benjamin Aaron Garcia3University of Pennsylvania School of MedicineUniversity of Pennsylvania School of MedicineUniversity of Pennsylvania School of MedicineUniversity of Pennsylvania School of MedicineHistone proteins are dynamically modified to mediate a variety of cellular processes including gene transcription, DNA damage repair, and apoptosis. Regulation of these processes occurs through the recruitment of non-histone proteins to chromatin by specific combinations of histone post-translational modifications (PTMs). Mass spectrometry has emerged as an essential tool to discover and quantify histone PTMs both within and between samples in an unbiased manner. Developments in mass spectrometry that allow for characterization of large histone peptides or intact protein has made it possible to determine which modifications occur simultaneously on a single histone polypeptide. A variety of techniques from biochemistry, biophysics, and chemical biology have been employed to determine the biological relevance of discovered combinatorial codes. This review first describes advancements in the field of mass spectrometry that have facilitated histone PTM analysis and then covers notable approaches to probe the biological relevance of these modifications in their nucleosomal context.http://journal.frontiersin.org/Journal/10.3389/fgene.2013.00264/fullChromatinHistone CodeMass SpectrometryProteomicshistonepost-translational modification |
| spellingShingle | Kelly R Karch Jamie E DeNizio Ben E Black Benjamin Aaron Garcia Identification and Interrogation of Combinatorial Histone Modifications Frontiers in Genetics Chromatin Histone Code Mass Spectrometry Proteomics histone post-translational modification |
| title | Identification and Interrogation of Combinatorial Histone Modifications |
| title_full | Identification and Interrogation of Combinatorial Histone Modifications |
| title_fullStr | Identification and Interrogation of Combinatorial Histone Modifications |
| title_full_unstemmed | Identification and Interrogation of Combinatorial Histone Modifications |
| title_short | Identification and Interrogation of Combinatorial Histone Modifications |
| title_sort | identification and interrogation of combinatorial histone modifications |
| topic | Chromatin Histone Code Mass Spectrometry Proteomics histone post-translational modification |
| url | http://journal.frontiersin.org/Journal/10.3389/fgene.2013.00264/full |
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