Journal
JOURNAL OF PROTEOME RESEARCH
Volume 7, Issue 10, Pages 4225-4236Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr800044q
Keywords
histone; post-translational modification; mass spectrometry; electron capture dissociation; variants; proteomic
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Funding
- NIGMS NIH HHS [1 F32 GM 078942-01, F32 GM078942, R01 GM067193-07, R01 GM067193, GM 067193, R01 GM067193-05] Funding Source: Medline
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Analyses of histone H3 from 10 rat tissues using a Middle Down proteomics platform revealed tissue-specific differences in their expression and global PTM abundance. ESI/FTMS with electron capture dissociation showed that, in general, these proteins were hypomodified in heart, liver and testes. H3.3 was hypermodified compared to H3.2 in some, but not all tissues. In addition, a novel rat testes-specific H3 protein was identified with this approach.
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