Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

Nature

Volumn 401, Issue 6748, 1999, Pages 93-98

  Rojas, Jeannie R ^a   Trievel, Raymond C ^a   Zhou, Jianxin ^b   Mo, Yi ^a   Li, Xinmin ^a   Berger, Shelley L ^a   Allis, C David ^b,c   Marmorstein, Ronen ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF ROCHESTER   (United States)

^c UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; HISTONE H3;

ARTICLE; BINDING SITE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TETRAHYMENA;

PROTOZOA; TETRAHYMENA;

EID: 0033517354     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/43487     Document Type: Article

References (29)

1. Grant, P. A., Sterner, D. E., Duggan, L. J., Workman, J. L. & Berger, S. L The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes. Trends Cell Biol. 8, 193-197 (1998).
2. Mizzen, C. A. & Allis, C. D. Linking histone acetylation to transcriptional regulation. Cell. Mol. Life Sci. 54, 6-20 (1998).
3. Trievel, R. C. et al. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl Acad. Sci. USA 96, 8931-8936 (1999).
4. Clements, A. et al. Crystal structure of the histone acetyltransferase domain of the human P/CAF transcriptional regulator bound to coenzyme-A. EMBO J. 18, 3521-3532 (1999).
5. Neuwald, A. F. & Landsman, D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that include the yeast SPT10 protein. Trends Biochem. Sci. 22, 154-155 (1997).
6. Dutnall, R. N., Tafrov, S. T., Sternglanz, R. & Ramakishnan, V. Structure of the histone acetyltransferase Hat I: A paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 94, 427-438 (1998).
7. Wolf, E. et al. Crystal structure of a GCN5-related N-acetyltransferase: Serratia maracescens aminoglycoside 3-N-acetyltransferase. Cell 94, 439-449 (1998).
8. Hickman, A., Namboodiri, M. A. A., Klein, D. C. & Dyda, F. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 Å resolution with a bisubstrate analog. Cell 97, 361-369 (1999).
9. Hickman, A. B., Klein, D. C. & Dyda, F. Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 angstrom resolution suggests a catalytic mechanism. Mol. Cell 3, 23-32 (1999).
10. Lin, Y., Fletcher, M., Zhou, J., Allis, C. D. & Wagner, G. Solution structure of the catalytic domain of Tetrahymena GCN5 histone acetyltransferase in complex with coenzyme A. Nature 400, 86-89 (1999).
11. Tanner, K. G. et al. Catalytic mechanism and function of invariant glutamic acid-173 from the histone acetyltransferase GCN5 transcriptional coactivator. J. Biol. Chem. 274, 18157-18160 (1999).
12. Kuo, M. H-, Zhou, J. X., Jambeck, P., Churchill, M. E. A. & Allis, C. D. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo. Genes Dev. 12, 627-639 (1998).
13. Wang, L., Liu, L. & Berger, S. L. Critical residues for histone acerylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo. Genes Dev. 12, 640-653 (1998).
14. Grant, P. A. et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev. 11, 1640-1650 (1997).
15. Grant, P. A. et al. Expanded lysine acetylation specificity of Gcn5 in native complexes. J. Biol. Chem. 274, 5895-5900 (1999).
16. Weston, S. A. et al. Crystal structure of the anti-fungal target N-myristoyltransferase. Nature Struct. Biol. 5, 213-221 (1998).
17. Bhatnagar, R. S. et al. Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs. Nature Struct. Biol. 5, 1091-1097 (1998).
18. Otwinowski, Z. in Proceedings of the CCP4 Study Weekend: Data collection and processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) 56-62 (SERC Daresbury Laboratory, Warrington, UK, 1993).
19. Leslie, A. G. W. in CCP4 and ESF-EACMB Newsletter on Protein Crystallography (Daresbury Laboratory, Daresbury, UK, 1992).
20. Furey, W. & Swaminathan, S. in Methods in Enzymology (eds Carter, C. W. & Sweet, R. M.) 590-620 (Academic, Orlando, 1997).
21. Jones, T. A., Zou, J. Y. & Cowen, S. W. 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).
22. Brunger, A. T. X-PLOR Manual, Version 3.8 (Yale Univ. Press, New Haven, 1996).
23. Brunger, A. T. & Krukowski, A. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A 46, 585-593 (1990).
24. Rice, L. M. & Brunger, A T. Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19, 277-290 (1994).
25. Jiang, J. S. & Brunger, A. T. Protein hydration observed in X-ray diffraction: solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115 (1994).
26. Brunger, A. T., Kuriyan, J. & Karplus, M. Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460 (1987).
27. Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
28. Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
29. Jones, T. A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallogr. 11, 268-272 (1978).