Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p

Journal of Molecular Biology

Volumn 349, Issue 3, 2005, Pages 608-620

  Sanderson, Andrew ^a   Stott, Katherine ^a   Stevens, Timothy J ^a   Thomas, Jean O ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Chromatin; Chromatosome; Intrinsically unstructured domain; NMR spectroscopy; Nucleosome

Indexed keywords

ALPHA GLUCOSIDASE AB; GLOBULAR PROTEIN; GLUCOSIDASE; GLUCOSIDASE I; HISTONE H1; MUTANT PROTEIN; SODIUM DIHYDROGEN PHOSPHATE; TYPE II SITE SPECIFIC DEOXYRIBONUCLEASE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CELL POPULATION; CELL PROTECTION; CONTROLLED STUDY; DNA BINDING; ENZYME ASSAY; ENZYME ENGINEERING; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; GENETIC CONSERVATION; GENETIC LINKAGE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; RESTRICTION SITE; SITE DIRECTED MUTAGENESIS; SUBSTITUTION REACTION; YEAST; YEAST ARTIFICIAL CHROMOSOME;

EID: 19444366667     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.03.085     Document Type: Article

References (31)

1. D. Landsman Histone H1 in Saccharomyces cerevisiae-a double mystery solved Trends Biochem. Sci. 21 1996 287 288
2. Y.-B. Zhou, S.E. Gerchmann, V. Ramakrishnan, A. Travers, and S. Muyldermans Position and orientation of the globular domain of linker histone H5 on the nucleosome Nature 395 1998 402 405
3. V. Ramakrishnan, J.T. Finch, V. Graziano, P.L. Lee, and R.M. Sweet Crystal structure of globular domain of histone H5 and its implications for nucleosome binding Nature 362 1993 219 223
4. F.A. Goytisolo, S.E. Gerchman, X. Yu, C. Rees, V. Graziano, V. Ramakrishnan, and J.O. Thomas Identification of two DNA-binding sites on the globular domain of histone H5 EMBO J. 15 1996 3421 3429
5. H.G. Patterton, C.C. Landel, D. Landsman, C.L. Peterson, and R.T. Simpson The biochemical and phenotypic characterization of Hho1p, the putative linker histone H1 of Saccharomyces cerevisiae J. Biol. Chem. 273 1998 7268 7276
6. T. Ali, and J.O. Thomas Distinct properties of the two putative "globular domains" of the yeast linker histone Hho1p J Mol. Biol. 337 2004 1123 1135
7. R.T. Simpson Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones Biochemistry 17 1978 5524 5531
8. J. Allan, P.G. Hartman, C. Crane-Robinson, and F.X. Aviles The structure of histone H1 and its location in chromatin Nature 288 1980 675 679
9. T. Ali, P. Coles, T.J. Stevens, K. Stott, and J.O. Thomas Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p J. Mol. Biol. 338 2004 139 148
10. C. Cerf, G. Lippens, V. Ramakrishnan, S. Muyldermans, A. Segers, and L. Wyns Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of H5 Biochemistry 33 1994 11079 11086
11. J.P. Linge, M. Habeck, W. Rieping, and M. Nilges ARIA: automated NOE assignment and NMR structure calculation Bioinformatics 19 2003 315 316
12. K. Ono, O. Kusano, S. Shimotakahara, M. Shimizu, T. Yamazaki, and H. Shindo The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged-helix-turn-helix fold as determined by NMR spectroscopy Nucl. Acids Res. 312 2003 7199 7207
13. G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
14. M.M. Duggan, and J.O. Thomas Two DNA-binding sites on the globular domain of histone H5 are required for binding to both bulk and 5 S reconstituted nucleosomes J. Mol. Biol. 304 2000 21 33
15. H.J. Dyson, and P.E. Wright Coupling of folding and binding for unstructured proteins Curr. Opin. Struct. Biol. 12 2002 54 60
16. J. Downs, E. Kosmidou, A. Morgan, and S.P. Jackson Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone Mol. Cell 11 2003 1685 1692
17. A. Harvey, and J. Downs What functions do linker histones provide? Mol. Microbiol. 53 2004 771 775
18. I. Freidkin, and D.J. Katcoff Specific distribution of the Saccharomyces cerevisiae linker histone homolog HHO1p in the chromatin Nucl. Acids Res. 29 2001 4043 4051
19. P.P. Nelson, S.C. Albright, J.M. Wiseman, and W.T. Garrard Reassociation of histone H1 with nucleosomes J. Biol. Chem. 254 1979 11751 11760
20. J.O. Thomas, and V. Furber Yeast chromatin structure FEBS Letters 66 1976 274 280
21. D. Lohr, R.T. Kovacic, and K.E. van Holde Quantitative analysis of the digestion of yeast chromatin by staphylococcal nuclease Biochemistry 16 1977 463 471
22. S. Perrin, and G. Gilliland Site-specific mutagenesis using asymmetric polymerase chain reaction and a single mutant primer Nucl. Acids Res. 18 1990 7433 7438
23. J. Cavanagh, W.J. Fairbrother, A.G. Palmer, and N.J. Skelton Protein NMR Spectroscopy: Principles and Practice 1996 Academic Press San Diego, CA, USA
24. 15N NMR relaxation Biochemistry 33 1994 5984 6003
25. 15N HSQC experiments optimized to retain full sensitivity J. Magn. Reson. Ser. A 102 1993 241 245
26. W.F. Vranken, W. Boucher, T.J. Stevens, R.H. Fogh, A. Pajon, and E. Ulrich The CCPN data model for NMR spectroscopy: development of a software pipeline for HTP projects Proteins: Struct. Funct. Genet 2005 [April 6, Epub ahead of print].
27. A.T. Brunger, P.D. Adams, G.M. Clore, W.L. DeLano, P. Gros, and R.W. Grosse-Kunstleve Crystallography and NMR system: a new software suite for macromolecular structure determination Acta Crystallog. Sect. D., Biol. Crystallog. 54 1998 905 921
28. R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
29. P.J. Kraulis MOLSCRIPT-a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
30. E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
31. R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 283 291