The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3
Open accessAbstract
Histone methylation has emerged as an important mechanism for regulating the transcriptional accessibility of chromatin. Several methyltransferases have been shown to target histone amino-terminal tails and mark nucleosomes associated with either euchromatic or heterochromatic states. However, the biochemical machinery responsible for regulating histone methylation and integrating it with other cellular events has not been well characterized. We report here the purification, molecular identification, and genetic and biochemical characterization of the Set1 protein complex that is necessary for methylation of histone H3 at lysine residue 4 in Saccharomyces cerevisiae . The seven-member 363-kDa complex contains homologs of Drosophila melanogaster proteins Ash2 and Trithorax and Caenorhabditis elegans protein DPY-30, which are implicated in the maintenance of Hox gene expression and regulation of X chromosome dosage compensation, respectively. Mutations of Set1 protein comparable to those that disrupt developmental function of its Drosophila homolog Trithorax abrogate histone methylation in yeast. These studies suggest that epigenetic regulation of developmental and sex-specific gene expression are species-specific readouts for a common chromatin remodeling machinery associated mechanistically with histone methylation.
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Cites
A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., et al. (2000) · Nature · doi:10.1038/35001009 · Cited by 4,706
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
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
Cited by
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,057
Carrozza, M. J., Li, B., Florens, L., Suganuma, T., Swanson, S. K., Lee, K. K., Shia, W.-J., Anderson, S., Yates, J., Washburn, M. P., et al. (2005) · Cell · doi:10.1016/j.cell.2005.10.023 · Cited by 1,294
Systematic Protein Location Mapping Reveals Five Principal Chromatin Types in Drosophila Cells
Filion, G. J., van Bemmel, J. G., Braunschweig, U., Talhout, W., Kind, J., Ward, L. D., Brugman, W., de Castro, I. J., Kerkhoven, R. M., Bussemaker, H. J., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.009 · Cited by 964
Histone methylation in transcriptional control
Kouzarides, T. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00287-3 · Cited by 908
The many faces of histone lysine methylation
Lachner, M., & Jenuwein, T. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00335-6 · Cited by 819
Metadata
- Authors
- Nagy, P. L., Griesenbeck, J., Kornberg, R. D., & Cleary, M. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-12-18
- Volume
- 99
- Issue
- 1
- Pages
- 90-94
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2070959297
- Cited by
- 311
- References
- 3
- FWCI
- 6.95
- Type
- journal article
- Language
- en
- Open access
- green
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- Nagy, P. L., Griesenbeck, J., Kornberg, R. D., & Cleary, M. L. (2002). A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.221596698
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