The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
In Vivo Residue-specific Histone Methylation Dynamics
Open accessAbstract
Methylation of specific histone residues is capable of both gene activation and silencing. Despite vast work on the function of methylation, most studies either present a static snapshot of methylation or fail to assign kinetic information to specific residues. Using liquid chromatography-tandem mass spectrometry on a high-resolution mass spectrometer and heavy methyl-SILAC labeling, we studied site-specific histone lysine and arginine methylation dynamics. The detection of labeled intermediates within a methylation state revealed that mono-, di-, and trimethylated residues generally have progressively slower rates of formation. Furthermore, methylations associated with active genes have faster rates than methylations associated with silent genes. Finally, the presence of both an active and silencing mark on the same peptide results in a slower rate of methylation than the presence of either mark alone. Here we show that quantitative proteomic approaches such as this can determine the dynamics of multiple methylated residues, an understudied portion of histone biology.
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Cites
1 retracted
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A bivalent chromatin structure marks key developmental genes in embryonic stem cells
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Cited by
The Polycomb complex PRC2 and its mark in life
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“Histone proteins are characterized by a high ratio of both lysine and arginine residues (Garcia et al., 2007a; Zee et al., 2010).”
BackgroundPotent inhibition of DOT1L as treatment of MLL-fusion leukemia
Daigle, S. R., Olhava, E. J., Therkelsen, C. A., Basavapathruni, A., Jin, L., Boriack-Sjodin, P. A., Allain, C. J., Klaus, C. R., Raimondi, A., Scott, M. P., et al. (2013) · Blood · doi:10.1182/blood-2013-04-497644 · Cited by 722
Influence of Threonine Metabolism on S -Adenosylmethionine and Histone Methylation
Shyh-Chang, N., Locasale, J. W., Lyssiotis, C. A., Zheng, Y., Teo, R. Y., Ratanasirintrawoot, S., Zhang, J., Onder, T., Unternaehrer, J. J., Zhu, H., et al. (2013) · Science · doi:10.1126/science.1226603 · Cited by 638
Metadata
- Authors
- Zee, B. M., Levin, R. S., Xu, B., LeRoy, G., Wingreen, N. S., & Garcia, B. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 285
- Issue
- 5
- Pages
- 3341-3350
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2047611070
- Cited by
- 260
- References
- 49
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Zee, B. M., Levin, R. S., Xu, B., LeRoy, G., Wingreen, N. S., & Garcia, B. A. (2010). In Vivo Residue-specific Histone Methylation Dynamics. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m109.063784
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