Solution Structure of the THAP Domain from Caenorhabditis elegans C-terminal Binding Protein (CtBP)

Journal of Molecular Biology

Volumn 366, Issue 2, 2007, Pages 382-390

  Liew, Chu Kong ^a   Crossley, Merlin ^a   Mackay, Joel P ^a   Nicholas, Hannah R ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

Author keywords

Caenorhabditis elegans; CtBP; NMR structure; THAP domain; zinc finger

Indexed keywords

BINDING PROTEIN; C TERMINAL BINDING PROTEIN; DOUBLE STRANDED DNA; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

ARTICLE; CAENORHABDITIS ELEGANS; CARBOXY TERMINAL SEQUENCE; DROSOPHILA; ELECTROPHORESIS; GEL MOBILITY SHIFT ASSAY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; ZINC FINGER MOTIF;

CAENORHABDITIS ELEGANS;

EID: 33846336737     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.058     Document Type: Article

References (36)

1. Turner J., and Crossley M. The CtBP family: enigmatic and enzymatic transcriptional co-repressors. BioEssays 23 (2001) 683-690
2. Shi Y., Sawada J., Sui G., Affar el B., Whetstine J.R., Lan F., et al. Coordinated histone modifications mediated by a CtBP co-repressor complex. Nature 422 (2003) 735-738
3. Shi Y., Lan F., Matson C., Mulligan P., Whetstine J.R., Cole P.A., and Casero R.A. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119 (2004) 941-953
4. Nibu Y., Zhang H., Bajor E., Barolo S., Small S., and Levine M. dCtBP mediates transcriptional repression by Knirps, Kruppel and Snail in the Drosophila embryo. EMBO J. 17 (1998) 7009-7020
5. Poortinga G., Watanabe M., and Parkhurst S.M. Drosophila CtBP: a Hairy-interacting protein required for embryonic segmentation and hairy-mediated transcriptional repression. EMBO J. 17 (1998) 2067-2078
6. Bergman L.M., and Blaydes J.P. C-terminal binding proteins: emerging roles in cell survival and tumorigenesis. Apoptosis 11 (2006) 879-888
7. Grooteclaes M., Deveraux Q., Hildebrand J., Zhang Q., Goodman R.H., and Frisch S.M. C-terminal-binding protein corepresses epithelial and proapoptotic gene expression programs. Proc. Natl Acad. Sci. USA 100 (2003) 4568-4573
8. Fjeld C.C., Birdsong W.T., and Goodman R.H. Differential binding of NAD+ and NADH allows the transcriptional corepressor carboxyl-terminal binding protein to serve as a metabolic sensor. Proc. Natl Acad. Sci. USA 100 (2003) 9202-9207
9. Nardini M., Svergun D., Konarev P.V., Spano S., Fasano M., Bracco C., et al. The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein Sci. 15 (2006) 1042-1050
10. Roussigne M., Kossida S., Lavigne A.C., Clouaire T., Ecochard V., Glories A., et al. The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase. Trends Biochem. Sci. 28 (2003) 66-69
11. Roussigne M., Cayrol C., Clouaire T., Amalric F., and Girard J.P. THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-response-4 (Par-4) to PML nuclear bodies. Oncogene 22 (2003) 2432-2442
12. Macfarlan T., Kutney S., Altman B., Montross R., Yu J., and Chakravarti D. Human THAP7 is a chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressor. J. Biol. Chem. 280 (2005) 7346-7358
13. Boxem M., and van den Heuvel S. C. elegans class B synthetic multivulva genes act in G(1) regulation. Curr. Biol. 12 (2002) 906-911
14. Reddy K.C., and Villeneuve A.M. C. elegans HIM-17 links chromatin modification and competence for initiation of meiotic recombination. Cell 118 (2004) 439-452
15. Clouaire T., Roussigne M., Ecochard V., Mathe C., Amalric F., and Girard J.P. The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity. Proc. Natl Acad. Sci. USA 102 (2005) 6907-6912
16. Pelton J.G., Torchia D.A., Meadow N.D., and Roseman S. Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci. 2 (1993) 543-558
17. Plesniak L.A., Connelly G.P., Wakarchuk W.W., and McIntosh L.P. Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange. Protein Sci. 5 (1996) 2319-2328
18. Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
19. Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
20. Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., and Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337 (2004) 635-645
21. Jauch R., Bourenkov G.P., Chung H.R., Urlaub H., Reidt U., Jackle H., and Wahl M.C. The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction module. Structure 11 (2003) 1393-1402
22. Grishin N.V. Treble clef finger-a functionally diverse zinc-binding structural motif. Nucl. Acids Res. 29 (2001) 1703-1714
23. Krishna S.S., Majumdar I., and Grishin N.V. Structural classification of zinc fingers: survey and summary. Nucl. Acids Res. 31 (2003) 532-550
24. Marti-Renom M.A., Stuart A.C., Fiser A., Sanchez R., Melo F., and Sali A. Comparative protein structure modeling of genes and genomes. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 291-325
25. Liew C.K., Simpson R.J., Kwan A.H., Crofts L.A., Loughlin F.E., Matthews J.M., et al. Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction. Proc. Natl Acad. Sci. USA 102 (2005) 583-588
26. Chesney M.A., Kidd III A.R., and Kimble J. gon-14 functions with class B and class C synthetic multivulva genes to control larval growth in Caenorhabditis elegans. Genetics 172 (2006) 915-928
27. Ferguson E.L., and Horvitz H.R. The multivulva phenotype of certain Caenorhabditis elegans mutants results from defects in two functionally redundant pathways. Genetics 123 (1989) 109-121
28. Siddiqui H., Solomon D.A., Gunawardena R.W., Wang Y., and Knudsen E.S. Histone deacetylation of RB-responsive promoters: requisite for specific gene repression but dispensable for cell cycle inhibition. Mol. Cell Biol. 23 (2003) 7719-7731
29. Katoh K., Kuma K., Toh H., and Miyata T. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucl. Acids Res. 33 (2005) 511-518
30. Clamp M., Cuff J., Searle S.M., and Barton G.J. The Jalview Java alignment editor. Bioinformatics 20 (2004) 426-427
31. Bond C.S. TopDraw: a sketchpad for protein structure topology cartoons. Bioinformatics 19 (2003) 311-312
32. Cai M., Huang Y., Sakaguchi K., Clore G.M., Gronenborn A.M., and Craigie R. An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11 (1998) 97-102
33. 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
34. 13C chemical shift statistics. J. Biomol. NMR 24 (2002) 149-154
35. Linge J.P., O'Donoghue S.I., and Nilges M. Automated assignment of ambiguous nuclear overhauser effects with ARIA. Methods Enzymol. 339 (2001) 71-90
36. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921