The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
A Human Protein Complex Homologous to the Drosophila MSL Complex Is Responsible for the Majority of Histone H4 Acetylation at Lysine 16
Open accessAbstract
We describe a stable, multisubunit human histone acetyltransferase complex (hMSL) that contains homologs of the Drosophila dosage compensation proteins MOF, MSL1, MSL2, and MSL3. This complex shows strong specificity for histone H4 lysine 16 in chromatin in vitro, and RNA interference-mediated knockdown experiments reveal that it is responsible for the majority of H4 acetylation at lysine 16 in the cell. We also find that hMOF is a component of additional complexes, forming associations with host cell factor 1 and a protein distantly related to MSL1 (hMSL1v1). We find two versions of hMSL3 in the hMSL complex that differ by the presence of the chromodomain. Lastly, we find that reduction in the levels of hMSLs and acetylation of H4 at lysine 16 are correlated with reduced transcription of some genes and with a G(2)/M cell cycle arrest. This is of particular interest given the recent correlation of global loss of acetylation of lysine 16 in histone H4 with tumorigenesis.
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Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome
Kornberg, R. D., & Lorch, Y. (1999) · Cell · doi:10.1016/s0092-8674(00)81958-3 · Cited by 1,830
Histones and histone modifications
Peterson, C. L., & Laniel, M.-A. (2004) · Current Biology · doi:10.1016/j.cub.2004.07.007 · Cited by 1,313
Structure of HP1 Chromodomain Bound to a Lysine 9-Methylated Histone H3 Tail
Jacobs, S. A., & Khorasanizadeh, S. (2002) · Science · doi:10.1126/science.1069473 · Cited by 832
Jeppesen, P., & Turner, B. M. (1993) · Cell · doi:10.1016/0092-8674(93)90419-q · Cited by 698
Dou, Y., Milne, T. A., Tackett, A. J., Smith, E. R., Fukuda, A., Wysocka, J., Allis, C. D., Chait, B. T., Hess, J. L., & Roeder, R. G. (2005) · Cell · doi:10.1016/j.cell.2005.04.031 · Cited by 664
Self-citationYokoyama, A., Wang, Z., Wysocka, J., Sanyal, M., Aufiero, D. J., Kitabayashi, I., Herr, W., & Cleary, M. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5639-5649.2004 · Cited by 662
Mapping Global Histone Acetylation Patterns to Gene Expression
Kurdistani, S. K., Tavazoie, S., & Grunstein, M. (2004) · Cell · doi:10.1016/j.cell.2004.05.023 · Cited by 647
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Self-citationStrahl, B. D., Grant, P. A., Briggs, S. D., Sun, Z.-W., Bone, J. R., Caldwell, J. A., Mollah, S., Cook, R. G., Shabanowitz, J., Hunt, D. F., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1298-1306.2002 · Cited by 562
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Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
Epigenetics and aging: the targets and the marks
Fraga, M. F., & Esteller, M. (2007) · Trends in Genetics · doi:10.1016/j.tig.2007.05.008 · Cited by 690
Thompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357
p53 Acetylation: Regulation and Consequences
Reed, S., & Quelle, D. (2014) · Cancers · doi:10.3390/cancers7010030 · Cited by 332
NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs
Vaquero, A., Sternglanz, R., & Reinberg, D. (2007) · Oncogene · doi:10.1038/sj.onc.1210617 · Cited by 296
Metadata
- Authors
- Smith, E. R., Cayrou, C., Huang, R., Lane, W. S., Côté, J., & Lucchesi, J. C.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2005-11-01
- Volume
- 25
- Issue
- 21
- Pages
- 9175-9188
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2116196682
- Cited by
- 334
- References
- 60
- FWCI
- 4.38
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: A Human Protein Complex Homologous to the Drosophila MSL Complex Is Responsible for the Majority of Histone H4 Acetylation at Lysine 16. https://app.cochat.ai/papers/10.1128/mcb.25.21.9175-9188.2005
- The paper
- Smith, E. R., Cayrou, C., Huang, R., Lane, W. S., Côté, J., & Lucchesi, J. C. (2005). A Human Protein Complex Homologous to the Drosophila MSL Complex Is Responsible for the Majority of Histone H4 Acetylation at Lysine 16. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.25.21.9175-9188.2005
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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