The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Mass spectrometry analysis of Arabidopsis histone H3 reveals distinct combinations of post-translational modifications
Open accessAbstract
Chromatin is regulated at many different levels, from higher-order packing to individual nucleosome placement. Recent studies have shown that individual histone modifications, and combinations thereof, play a key role in modulating chromatin structure and gene activity. Reported here is an analysis of Arabidopsis histone H3 modifications by nanoflow-HPLC coupled to electrospray ionization on a hybrid linear ion trap-Fourier transform mass spectrometer (LTQ/FTMS). We find that the sites of acetylation and methylation, in general, correlate well with other plants and animals. Two well-studied modifications, dimethylation of Lys-9 (correlated with silencing) and acetylation of Lys-14 (correlated with active chromatin) while abundant by themselves were rarely found on the same histone H3 tail. In contrast, dimethylation at Lys-27 and monomethylation at Lys-36 were commonly found together. Interestingly, acetylation at Lys-9 was found only in a low percentage of histones while acetylation of Lys-14 was very abundant. The two histone H3 variants, H3.1 and H3.2, also differ in the abundance of silencing and activating marks confirming other studies showing that the replication-independent histone H3 is enriched in active chromatin.
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Cites
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845
From Silencing to Gene Expression
Janicki, S. M., Tsukamoto, T., Salghetti, S. E., Tansey, W. P., Sachidanandam, R., Prasanth, K. V., Ried, T., Shav-Tal, Y., Bertrand, E., Singer, R. H., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00171-0 · Cited by 704
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
Kuo, M.-H., Brownell, J. E., Sobel, R. E., Ranalli, T. A., Cook, R. G., Edmondson, D. G., Roth, S. Y., & Allis, C. D. (1996) · Nature · doi:10.1038/383269a0 · Cited by 596
Cited by
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902
Whole-Genome Analysis of Histone H3 Lysine 27 Trimethylation in Arabidopsis
Zhang, X., Clarenz, O., Cokus, S., Bernatavichute, Y. V., Pellegrini, M., Goodrich, J., & Jacobsen, S. E. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050129 · Cited by 767
Chromatin immunoprecipitation: optimization, quantitative analysis and data normalization
Haring, M., Offermann, S., Danker, T., Horst, I., Peterhansel, C., & Stam, M. (2007) · Plant Methods · doi:10.1186/1746-4811-3-11 · Cited by 508
Kim, J.-M., To, T. K., Ishida, J., Morosawa, T., Kawashima, M., Matsui, A., Toyoda, T., Kimura, H., Shinozaki, K., & Seki, M. (2008) · Plant and Cell Physiology · doi:10.1093/pcp/pcn133 · Cited by 346
Azizi, P., Hanafi, M. M., Sahebi, M., Harikrishna, J. A., Taheri, S., Yassoralipour, A., & Nasehi, A. (2020) · Functional Plant Biology · doi:10.1071/fp19077 · Cited by 46
Metadata
- Authors
- Johnson, L.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2004-12-14
- Volume
- 32
- Issue
- 22
- Pages
- 6511-6518
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2138248567
- Cited by
- 252
- References
- 4
- FWCI
- 5.14
- Type
- journal article
- Language
- en
- Open access
- bronze
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