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Proceedings of the National Academy of Sciences of the United States of America
Apr 26, 2005;102 (17): 5975-80.

Structural basis for the interaction of Asf1 with histone H3 and its functional implications.

Florence Mousson, Aurélie Lautrette, Jean-Yves Thuret, Morgane Agez, Régis Courbeyrette, Béatrice Amigues, Emmanuelle Becker, Jean-Michel Neumann, Raphaël Guerois, Carl Mann, Françoise Ochsenbein
Author Information
  1. Florence Mousson: Service de Biophysique des Fonctions Membranaires and Service de Biochimie et de Génétique Moléculaire, Département de Biologie Joliot-Curie, Commissariat à l'Energie Atomique (CEA/Saclay), F-91191 Gif-sur-Yvette, France.
PMID: 15840725 DOI: 10.1073/pnas.0500149102

Abstract

Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing.

Associated Data

PDB | 1TEY

References

  1. Annu Rev Biochem. 2003;72:481-516 [PMID: 12676793]
  2. J Biol Chem. 2003 Aug 15;278(33):31319-24 [PMID: 12791680]
  3. Curr Biol. 2003 Dec 16;13(24):2148-58 [PMID: 14680630]
  4. Cell. 2004 Jan 9;116(1):51-61 [PMID: 14718166]
  5. Mol Cell. 2004 Feb 13;13(3):307-16 [PMID: 14967139]
  6. Mol Cell Biol. 2004 Mar;24(6):2560-72 [PMID: 14993292]
  7. Biochim Biophys Acta. 2004 Mar 15;1677(1-3):3-11 [PMID: 15020040]
  8. J Biomol NMR. 2004 Jul;29(3):413-4 [PMID: 15213445]
  9. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5000-4 [PMID: 291918]
  10. Biochemistry. 1992 Feb 18;31(6):1647-51 [PMID: 1737021]
  11. J Biomol NMR. 1994 Mar;4(2):193-200 [PMID: 8019134]
  12. Proc Natl Acad Sci U S A. 1996 Jul 23;93(15):7588-93 [PMID: 8755519]
  13. Nat Struct Biol. 1996 Dec;3(12):995-7 [PMID: 8946851]
  14. J Mol Biol. 1997 Jun 13;269(3):408-22 [PMID: 9199409]
  15. Nature. 1997 Sep 18;389(6648):251-60 [PMID: 9305837]
  16. Genetics. 1998 Oct;150(2):613-32 [PMID: 9755194]
  17. J Biomol NMR. 1999 Mar;13(3):289-302 [PMID: 10212987]
  18. J Biol Chem. 2004 Dec 10;279(50):52069-74 [PMID: 15452122]
  19. Nature. 1999 Dec 2;402(6761):555-60 [PMID: 10591219]
  20. Genes Cells. 2000 Mar;5(3):221-33 [PMID: 10759893]
  21. Genes Dev. 2000 Jun 15;14(12):1430-8 [PMID: 10859162]
  22. Mol Cell. 2001 Jan;7(1):13-20 [PMID: 11172707]
  23. Genes Dev. 2001 May 1;15(9):1061-6 [PMID: 11331602]
  24. Genetics. 2001 Jun;158(2):587-96 [PMID: 11404324]
  25. Methods. 2001 Jul;24(3):218-29 [PMID: 11403571]
  26. Curr Biol. 2001 Apr 3;11(7):463-73 [PMID: 11412995]
  27. Curr Biol. 2001 Jul 10;11(13):1068-73 [PMID: 11470414]
  28. Proc Natl Acad Sci U S A. 2001 Aug 28;98(18):10037-41 [PMID: 11517324]
  29. Mol Cell Biol. 2001 Oct;21(19):6574-84 [PMID: 11533245]
  30. Genes Dev. 2001 Dec 1;15(23):3155-68 [PMID: 11731479]
  31. Genes Dev. 2001 Dec 1;15(23):3169-82 [PMID: 11731480]
  32. Mol Cell Biol. 2002 Jan;22(2):614-25 [PMID: 11756556]
  33. Genes Cells. 2002 Jan;7(1):59-73 [PMID: 11856374]
  34. EMBO Rep. 2002 Apr;3(4):329-34 [PMID: 11897662]
  35. Bioinformatics. 2002;18 Suppl 1:S71-7 [PMID: 12169533]
  36. Genes Dev. 2002 Oct 15;16(20):2621-6 [PMID: 12381660]
  37. Trends Cell Biol. 2002 Nov;12(11):509-16 [PMID: 12446112]
  38. Bioinformatics. 2003 Jan 22;19(2):315-6 [PMID: 12538267]
  39. Curr Opin Struct Biol. 2003 Feb;13(1):6-14 [PMID: 12581654]
  40. J Biol Chem. 2003 Nov 7;278(45):44574-83 [PMID: 12928440]

MeSH Term

Animals
Binding Sites
Cell Cycle Proteins
Chickens
Glutathione Transferase
Histones
Humans
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Chaperones
Mutagenesis, Site-Directed
Protein Conformation
Protein Structure, Secondary
Recombinant Fusion Proteins
Recombinant Proteins

Chemicals

ASF1A protein, human
Cell Cycle Proteins
Histones
Molecular Chaperones
Recombinant Fusion Proteins
Recombinant Proteins
Glutathione Transferase
Journal Article Research Support, Non-U.S. Gov't
Article has an altmetric score of 7

Word Cloud

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