메뉴 건너뛰기




Volumn 16, Issue 8, 2008, Pages 1245-1256

Structural Insight into the Recognition of the H3K4me3 Mark by the TFIID Subunit TAF3

Author keywords

DNA; PROTEIN

Indexed keywords

ARGININE; HISTONE H3; LYSINE; PROTEIN H3K4ME3; PROTEIN TAF3; TRANSCRIPTION FACTOR IID;

EID: 48149105342     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.04.015     Document Type: Article
Times cited : (108)

References (58)
  • 3
    • 30944452960 scopus 로고    scopus 로고
    • The PHD finger, a nuclear protein-interaction domain
    • Bienz M. The PHD finger, a nuclear protein-interaction domain. Trends Biochem. Sci. 31 (2006) 35-40
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 35-40
    • Bienz, M.1
  • 4
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan M.V., Lee J., Ward I.M., Kim J.E., Thompson J.R., Chen J.J., and Mer G. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127 (2006) 1361-1373
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5    Chen, J.J.6    Mer, G.7
  • 6
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 9
    • 48149099693 scopus 로고    scopus 로고
    • DeLano Scientific LLC (2008). PyMOL (http://www.pymol.org).
    • DeLano Scientific LLC (2008). PyMOL (http://www.pymol.org).
  • 10
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: a protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C., Boelens R., and Bonvin A.M. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125 (2003) 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 11
    • 0030043489 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
    • Dougherty D.A. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271 (1996) 163-168
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 12
    • 0035281284 scopus 로고    scopus 로고
    • Quantum/classical mechanical comparison of cation-π interactions between tetramethylammonium and benzene
    • Felder C., Jiang H.L., Zhu W.L., Chen K.X., Silman I., Botti S.A., and Sussman J.L. Quantum/classical mechanical comparison of cation-π interactions between tetramethylammonium and benzene. J. Phys. Chem. A 105 (2001) 1326-1333
    • (2001) J. Phys. Chem. A , vol.105 , pp. 1326-1333
    • Felder, C.1    Jiang, H.L.2    Zhu, W.L.3    Chen, K.X.4    Silman, I.5    Botti, S.A.6    Sussman, J.L.7
  • 13
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W., Wang Y.M., and Allis C.D. Binary switches and modification cassettes in histone biology and beyond. Nature 425 (2003) 475-479
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.M.2    Allis, C.D.3
  • 18
    • 34447098370 scopus 로고    scopus 로고
    • A chromatin landmark and transcription initiation at most promoters in human cells
    • Guenther M.G., Levine S.S., Boyer L.A., Jaenisch R., and Young R.A. A chromatin landmark and transcription initiation at most promoters in human cells. Cell 130 (2007) 77-88
    • (2007) Cell , vol.130 , pp. 77-88
    • Guenther, M.G.1    Levine, S.S.2    Boyer, L.A.3    Jaenisch, R.4    Young, R.A.5
  • 19
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 21
    • 34249757710 scopus 로고
    • Determination of the rotational-dynamics and pH-dependence of the hydrogen-exchange rates of the arginine guanidino group using Nmr-spectroscopy
    • Henry G.D., and Sykes B.D. Determination of the rotational-dynamics and pH-dependence of the hydrogen-exchange rates of the arginine guanidino group using Nmr-spectroscopy. J. Biomol. NMR 6 (1995) 59-66
    • (1995) J. Biomol. NMR , vol.6 , pp. 59-66
    • Henry, G.D.1    Sykes, B.D.2
  • 22
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319 (2002) 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 24
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y., Fang J., Bedford M.T., Zhang Y., and Xu R.M. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312 (2006) 748-751
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 25
    • 34547161846 scopus 로고    scopus 로고
    • Effects of chain length and N-methylation on a cation-π interaction in a β-hairpin peptide
    • Hughes R.M., Benshoff M.L., and Waters M.L. Effects of chain length and N-methylation on a cation-π interaction in a β-hairpin peptide. Chemistry (Easton) 13 (2007) 5753-5764
    • (2007) Chemistry (Easton) , vol.13 , pp. 5753-5764
    • Hughes, R.M.1    Benshoff, M.L.2    Waters, M.L.3
  • 26
    • 34547427285 scopus 로고    scopus 로고
    • Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect
    • Hughes R.M., Wiggins K.R., Khorasanizadeh S., and Waters M.L. Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect. Proc. Natl. Acad. Sci. USA 104 (2007) 11184-11188
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11184-11188
    • Hughes, R.M.1    Wiggins, K.R.2    Khorasanizadeh, S.3    Waters, M.L.4
  • 28
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs S.A., and Khorasanizadeh S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295 (2002) 2080-2083
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 29
    • 4644234334 scopus 로고    scopus 로고
    • Mars-robust automatic backbone assignment of proteins
    • Jung Y.S., and Zweckstetter M. Mars-robust automatic backbone assignment of proteins. J. Biomol. NMR 30 (2004) 11-23
    • (2004) J. Biomol. NMR , vol.30 , pp. 11-23
    • Jung, Y.S.1    Zweckstetter, M.2
  • 31
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 128 (2007) 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 33
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 34
    • 37849015924 scopus 로고    scopus 로고
    • Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
    • Lee J., Thompson J.R., Botuyan M.V., and Mer G. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat. Struct. Mol. Biol. 15 (2008) 109-111
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 109-111
    • Lee, J.1    Thompson, J.R.2    Botuyan, M.V.3    Mer, G.4
  • 35
    • 36249026356 scopus 로고    scopus 로고
    • Structural basis for lower lysine methylation state-specific readout by MBT repeats of L3MBTL1 and an engineered PHD finger
    • Li H., Fischle W., Wang W., Duncan E.M., Liang L., Murakami-Ishibe S., Allis C.D., and Patel D.J. Structural basis for lower lysine methylation state-specific readout by MBT repeats of L3MBTL1 and an engineered PHD finger. Mol. Cell 28 (2007) 677-691
    • (2007) Mol. Cell , vol.28 , pp. 677-691
    • Li, H.1    Fischle, W.2    Wang, W.3    Duncan, E.M.4    Liang, L.5    Murakami-Ishibe, S.6    Allis, C.D.7    Patel, D.J.8
  • 36
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • Li H.T., Ilin S., Wang W.K., Duncan E.M., Wysocka J., Allis C.D., and Patel D.J. Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442 (2006) 91-95
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.T.1    Ilin, S.2    Wang, W.K.3    Duncan, E.M.4    Wysocka, J.5    Allis, C.D.6    Patel, D.J.7
  • 38
    • 0033544354 scopus 로고    scopus 로고
    • Cation-π interactions in proteins: can simple models provide an accurate description?
    • Minoux H., and Chipot C. Cation-π interactions in proteins: can simple models provide an accurate description?. J. Am. Chem. Soc. 121 (1999) 10366-10372
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10366-10372
    • Minoux, H.1    Chipot, C.2
  • 41
    • 0034671463 scopus 로고    scopus 로고
    • Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor
    • Pascual J., Martinez-Yamout M., Dyson H.J., and Wright P.E. Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor. J. Mol. Biol. 304 (2000) 723-729
    • (2000) J. Mol. Biol. , vol.304 , pp. 723-729
    • Pascual, J.1    Martinez-Yamout, M.2    Dyson, H.J.3    Wright, P.E.4
  • 42
    • 35148851120 scopus 로고    scopus 로고
    • Binding of organic cations to gramicidin A channel studied with AutoDock and molecular dynamics simulations
    • Patra S.M., Bastug T., and Kuyucak S. Binding of organic cations to gramicidin A channel studied with AutoDock and molecular dynamics simulations. J. Phys. Chem. B 111 (2007) 11303-11311
    • (2007) J. Phys. Chem. B , vol.111 , pp. 11303-11311
    • Patra, S.M.1    Bastug, T.2    Kuyucak, S.3
  • 45
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark
    • Ruthenburg A.J., Allis C.D., and Wysocka J. Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Mol. Cell 25 (2007) 15-30
    • (2007) Mol. Cell , vol.25 , pp. 15-30
    • Ruthenburg, A.J.1    Allis, C.D.2    Wysocka, J.3
  • 48
    • 84962352816 scopus 로고    scopus 로고
    • 2+ interactions: thiol vs. thiolate coordination
    • 2+ interactions: thiol vs. thiolate coordination. Proteins 49 (2002) 37-48
    • (2002) Proteins , vol.49 , pp. 37-48
    • Simonson, T.1    Calimet, N.2
  • 49
    • 33751116960 scopus 로고    scopus 로고
    • Histone H3 Lys 4 methylation: caught in a bind?
    • Sims R.J., and Reinberg D. Histone H3 Lys 4 methylation: caught in a bind?. Genes Dev. 20 (2006) 2779-2786
    • (2006) Genes Dev. , vol.20 , pp. 2779-2786
    • Sims, R.J.1    Reinberg, D.2
  • 50
    • 29644433964 scopus 로고    scopus 로고
    • Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains
    • Sims R.J., Chen C.F., Santos-Rosa H., Kouzarides T., Patel S.S., and Reinberg D. Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains. J. Biol. Chem. 280 (2005) 41789-41792
    • (2005) J. Biol. Chem. , vol.280 , pp. 41789-41792
    • Sims, R.J.1    Chen, C.F.2    Santos-Rosa, H.3    Kouzarides, T.4    Patel, S.S.5    Reinberg, D.6
  • 51
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 52
    • 33751527233 scopus 로고    scopus 로고
    • Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
    • Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H.T., Baker L., Boyle J., Blair L.P., Chait B.T., et al. Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol. Cell 24 (2006) 785-796
    • (2006) Mol. Cell , vol.24 , pp. 785-796
    • Taverna, S.D.1    Ilin, S.2    Rogers, R.S.3    Tanny, J.C.4    Lavender, H.5    Li, H.T.6    Baker, L.7    Boyle, J.8    Blair, L.P.9    Chait, B.T.10
  • 55
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart D.S., and Sykes B.D. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4 (1994) 171-180
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 58
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage lambda N-peptide/boxB RNA complex
    • Zwahlen C., Legault P., Vincent S.J.F., Greenblatt J., Konrat R., and Kay L.E. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage lambda N-peptide/boxB RNA complex. J. Am. Chem. Soc. 119 (1997) 6711-6721
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.