期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 104, 期 7, 页码 2086-2091出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0610993104
关键词
bivalent domain; electron transfer dissociation; mass spectrometry; posttranslational modifications; Tetrahymena
资金
- NCRR NIH HHS [RR00862, RR022220, P41 RR000862, U54 RR022220] Funding Source: Medline
- NIGMS NIH HHS [R37 GM053512, GM53512, R01 GM063959, GM63959, R01 GM037537, GM37537] Funding Source: Medline
Individual posttranslational modifications (PTMs) on histones have well established roles in certain biological processes, notably transcriptional programming. Recent genomewide studies describe patterns of covalent modifications, such as H3 methylation and acetylation at promoters of specific target genes, or bivalent domains, in stem cells, suggestive of a possible combinatorial interplay between PTMs on the same histone. However, detection of long-range PTM associations is often problematic in antibody-based or traditional mass spectrometric-based analyses. Here, histone H3 from a ciliate model was analyzed as an enriched source of transcriptionally active chromatin. Using a recently developed mass spectrometric approach, combinatorial modification states on single, long N-terminal H3 fragments (residues 1-50) were determined. The entire modification status of intact N termini was obtained and indicated correlations between K4 methylation and H3 acetylation. In addition, K4 and K27 methylation were identified concurrently on one H3 species. This methodology is applicable to other histones and larger polypepticles and will likely be a valuable tool in understanding the roles of combinatorial patterns of PTMs.
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