Tissue-specific expression and post-translational modification of histone H3 variants

Benjamin A. Garcia; C. Eric Thomas; Neil L. Kelleher; Craig A. Mizzen

doi:10.1021/pr800044q

Tissue-specific expression and post-translational modification of histone H3 variants

Benjamin A. Garcia, C. Eric Thomas, Neil L. Kelleher, Craig A. Mizzen

Research output: Contribution to journal › Article › peer-review

58 Scopus citations

Abstract

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 rattestes-specific H3 protein was identified with this approach.

Original language	English
Pages (from-to)	4225-4236
Number of pages	12
Journal	Journal of Proteome Research
Volume	7
Issue number	10
DOIs	https://doi.org/10.1021/pr800044q
State	Published - Oct 2008

Keywords

Electron capture dissociation
Histone
Mass spectrometry
Post-translational modification
Proteomic
Variants

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10.1021/pr800044q

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abstract = "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 rattestes-specific H3 protein was identified with this approach.",

keywords = "Electron capture dissociation, Histone, Mass spectrometry, Post-translational modification, Proteomic, Variants",

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AU - Thomas, C. Eric

AU - Kelleher, Neil L.

AU - Mizzen, Craig A.

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Y1 - 2008/10

N2 - 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 rattestes-specific H3 protein was identified with this approach.

AB - 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 rattestes-specific H3 protein was identified with this approach.

KW - Electron capture dissociation

KW - Histone

KW - Mass spectrometry

KW - Post-translational modification

KW - Proteomic

KW - Variants

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U2 - 10.1021/pr800044q

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EP - 4236

JO - Journal of Proteome Research

JF - Journal of Proteome Research

IS - 10

ER -

Tissue-specific expression and post-translational modification of histone H3 variants

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Keywords

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