Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
10.1038/nature04814
Crossref journal-article
Springer Science and Business Media LLC
Nature (297)
Bibliography

Peña, P. V., Davrazou, F., Shi, X., Walter, K. L., Verkhusha, V. V., Gozani, O., Zhao, R., & Kutateladze, T. G. (2006). Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature, 442(7098), 100–103.

Authors 8
  1. Pedro V. Peña (first)
  2. Foteini Davrazou (additional)
  3. Xiaobing Shi (additional)
  4. Kay L. Walter (additional)
  5. Vladislav V. Verkhusha (additional)
  6. Or Gozani (additional)
  7. Rui Zhao (additional)
  8. Tatiana G. Kutateladze (additional)
References 27 Referenced 567
  1. Santos-Rosa, H. et al. Active genes are tri-methylated at K4 of histone H3. Nature 419, 407–411 (2002) (10.1038/nature01080) / Nature by H Santos-Rosa (2002)
  2. Schneider, R. et al. Histone H3 lysine 4 methylation patterns in higher eukaryotic genes. Nature Cell Biol. 6, 73–77 (2004) (10.1038/ncb1076) / Nature Cell Biol. by R Schneider (2004)
  3. Briggs, S. D. et al. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 15, 3286–3295 (2001) (10.1101/gad.940201) / Genes Dev. by SD Briggs (2001)
  4. Sims, R. J. III, Nishioka, K. & Reinberg, D. Histone lysine methylation: a signature for chromatin function. Trends Genet. 19, 629–639 (2003) (10.1016/j.tig.2003.09.007) / Trends Genet. by RJ Sims III (2003)
  5. Shi, X. et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature doi:10.1038/nature04835 (2006). (10.1038/nature04835)
  6. Strahl, B. D. & Allis, C. D. The language of covalent histone modifications. Nature 403, 41–45 (2000) (10.1038/47412) / Nature by BD Strahl (2000)
  7. Dhalluin, C. et al. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399, 491–496 (1999) (10.1038/20974) / Nature by C Dhalluin (1999)
  8. Jacobson, R. H., Ladurner, A. G., King, D. S. & Tjian, R. Structure and function of a human TAFII250 double bromodomain module. Science 288, 1422–1425 (2000) (10.1126/science.288.5470.1422) / Science by RH Jacobson (2000)
  9. Bannister, A. J. et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410, 120–124 (2001) (10.1038/35065138) / Nature by AJ Bannister (2001)
  10. Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410, 116–120 (2001) (10.1038/35065132) / Nature by M Lachner (2001)
  11. Nielsen, P. R. et al. Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. Nature 416, 103–107 (2002) (10.1038/nature722) / Nature by PR Nielsen (2002)
  12. Jacobs, S. A. & Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080–2083 (2002) (10.1126/science.1069473) / Science by SA Jacobs (2002)
  13. Flanagan, J. F. et al. Double chromodomains cooperate to recognize the methylated histone H3 tail. Nature 438, 1181–1185 (2005) (10.1038/nature04290) / Nature by JF Flanagan (2005)
  14. Ragvin, A. et al. Nucleosome binding by the bromodomain and PHD finger of the transcriptional cofactor p300. J. Mol. Biol. 337, 773–788 (2004) (10.1016/j.jmb.2004.01.051) / J. Mol. Biol. by A Ragvin (2004)
  15. Eberharter, A., Vetter, I., Ferreira, R. & Becker, P. B. ACF1 improves the effectiveness of nucleosome mobilization by ISWI through PHD-histone contacts. EMBO J. 23, 4029–4039 (2004) (10.1038/sj.emboj.7600382) / EMBO J. by A Eberharter (2004)
  16. Pascual, J., Martinez-Yamout, M., Dyson, H. J. & Wright, P. E. Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor. J. Mol. Biol. 304, 723–729 (2000) (10.1006/jmbi.2000.4308) / J. Mol. Biol. by J Pascual (2000)
  17. Fischle, W. et al. Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev. 17, 1870–1881 (2003) (10.1101/gad.1110503) / Genes Dev. by W Fischle (2003)
  18. Min, J., Zhang, Y. & Xu, R. M. Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 17, 1823–1828 (2003) (10.1101/gad.269603) / Genes Dev. by J Min (2003)
  19. Nagashima, M. et al. DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53. Proc. Natl Acad. Sci. USA 98, 9671–9676 (2001) (10.1073/pnas.161151798) / Proc. Natl Acad. Sci. USA by M Nagashima (2001)
  20. Doyon, Y. et al. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol. Cell 21, 51–64 (2006) (10.1016/j.molcel.2005.12.007) / Mol. Cell by Y Doyon (2006)
  21. Campos, E. I., Chin, M. Y., Kuo, W. H. & Li, G. Biological functions of the ING family tumor suppressors. Cell. Mol. Life Sci. 61, 2597–2613 (2004) (10.1007/s00018-004-4199-4) / Cell. Mol. Life Sci. by EI Campos (2004)
  22. Loewith, R., Meijer, M., Lees-Miller, S. P., Riabowol, K. & Young, D. Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol. Cell. Biol. 20, 3807–3816 (2000) (10.1128/MCB.20.11.3807-3816.2000) / Mol. Cell. Biol. by R Loewith (2000)
  23. Kuzmichev, A., Zhang, Y., Erdjument-Bromage, H., Tempst, P. & Reinberg, D. Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1). Mol. Cell. Biol. 22, 835–848 (2002) (10.1128/MCB.22.3.835-848.2002) / Mol. Cell. Biol. by A Kuzmichev (2002)
  24. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997) (10.1016/S0076-6879(97)76066-X) / Methods Enzymol. by Z Otwinowski (1997)
  25. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 (1991) (10.1107/S0108767390010224) / Acta Crystallogr. A by TA Jones (1991)
  26. Brünger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905–921 (1998) (10.1107/S0907444998003254) / Acta Crystallogr. D by AT Brünger (1998)
  27. Grzesiek, S., Stahl, S. J., Wingfield, P. T. & Bax, A. The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR. Biochemistry 35, 10256–10261 (1996) (10.1021/bi9611164) / Biochemistry by S Grzesiek (1996)
Dates
Type When
Created 19 years, 2 months ago (May 25, 2006, 1:39 p.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 1:55 p.m.)
Indexed 2 weeks, 2 days ago (Aug. 6, 2025, 8:17 a.m.)
Issued 19 years, 3 months ago (May 21, 2006)
Published 19 years, 3 months ago (May 21, 2006)
Published Online 19 years, 3 months ago (May 21, 2006)
Published Print 19 years, 1 month ago (July 1, 2006)
Funders 0

None

@article{Pe_a_2006, title={Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2}, volume={442}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature04814}, DOI={10.1038/nature04814}, number={7098}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Peña, Pedro V. and Davrazou, Foteini and Shi, Xiaobing and Walter, Kay L. and Verkhusha, Vladislav V. and Gozani, Or and Zhao, Rui and Kutateladze, Tatiana G.}, year={2006}, month=may, pages={100–103} }