Solution structure of the interacting domains of the mad-sin3 complex: Implications for recruitment of a chromatin-modifying complex

Cell

Volumn 103, Issue 4, 2000, Pages 655-665

  Brubaker, Kurt ^a   Cowley, Shaun M ^b   Huang, Kai ^a   Loo, Lenora ^b   Yochum, Gregory S ^c   Ayer, Donald E ^c   Eisenman, Robert N ^b   Radhakrishnan, Ishwar ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b Fred Hutchinson Cancer Research Center   (United States)

^c UNIVERSITY OF UTAH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR;

ARTICLE; CHROMATIN; CIRCULAR DICHROISM; COMPLEX FORMATION; DNA BINDING; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL;

ESCHERICHIA COLI; EUKARYOTA; MAMMALIA;

EID: 0033696968     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)00168-9     Document Type: Article

References (59)

1. NuRD and Sin3 histone deacetylase complexes in development
2. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression
3. 15N with side chain H(β) resonances in larger proteins
4. Histone deacetylases: Transcriptional repression with SlNers and NuRDs
5. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3
6. Mad proteins contain a dominant transcription repression domain
7. Methodological advances in protein NMR
8. Activation of RNA polymerase II transcription
9. Crystallography and NMR system (CNS): A new software system for macromolecular structure determination
10. A transcriptional corepressor that interacts with nuclear hormone receptors
11. Multidimensional heteronuclear nuclear magnetic resonance of proteins
12. Protein backbone angle restraints from searching a database for chemical shift and sequence homology
13. Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein
14. Structure and ligand of a histone acetyltransferase bromodomain
15. A 13-amino acid amphipathic α-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A
16. 15N NMR relaxation
17. Treatment of NOE constraints involving equivalent or non-stereoassigned protons in calculations of biomacromolecular structures
18. The corepressor mSin3A is a functional component of the REST-CoREST repressor complex
19. Multiplequantum line narrowing for measurement of H(α)-H(α) J couplings in isotopically enriched proteins
20. Torsion angle dynamics for NMR structure calculation with the new program DY-ANA
21. Histone deacetylase activity is required for full transcription repression by mSin3A
22. A complex containing N-CoR, rosin3 and histone deacetylase mediates transcriptional repression
23. Mapping the protein universe
24. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor corepressor
25. Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites
26. PROMOTIF-a program to identify and analyze structural motifs in proteins
27. Structure and function of a human TAF(III)250 double bromodomain module
28. Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription
29. Sin meets NuRD and other tails of repression
30. Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes
31. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
32. Measurement of H(N)-H(α) J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
33. Histone deacetylases associated with the Sin3 corepressor mediate Mad transcriptional repression
34. SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors
35. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
36. 13C-labeled proteins
37. 5 at 2.8 A resolution
38. Satisfying hydrogen bonding potential in proteins
39. Raster3D: Photorealistic molecular graphics
40. Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3A
41. SCOP: A structural classification of proteins database for the investigation of sequences and structures
42. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
43. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
44. Neural restrictive silencer factor recruits mSin3 and histone deacetylase complex to repress neuron-specific target genes
45. Histone deacetylases: Silencers for hire
46. Protein folding and association: Insights from the interracial and thermodynamic properties of hydrocarbons
47. Ski is a component of the histone deacetylase complex required for transcriptional repression by Mad and thyroid hormone receptor
48. Peptide velcrodesign of a heterodimeric coiled-coil
49. 1H]-NMR spectroscopy: Combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions
50. Transcriptional activation by recruitment
51. Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: Implications for the mapping of structural domains
52. Reduced surface: An efficient way to compute molecular surfaces
53. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor Sin3
54. 13C
55. The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs
56. 13C-labeled proteins via scalar couplings
57. The winged-helix/forkhead protein myocyte nuclear factor β (MNF-β) forms a corepressor complex with mammalian Sin3B
58. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
59. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage λ N-peptide/boxB RNA complex