The H3-H4 N-terminal tail domains are the primary mediators of transcription factor IIIA access to 5S DNA within a nucleosome

Molecular and Cellular Biology

Volumn 20, Issue 6, 2000, Pages 2167-2175

  Vitolo, Joseph M ^a   Thiriet, Christophe ^a   Hayes, Jeffrey J ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; HISTONE; NUCLEOPROTEIN; TETRAMER; TRANSCRIPTION FACTOR;

ACETYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; DNA CONTENT; DNA HISTONE INTERACTION; DNA SEQUENCE; NUCLEOSOME; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BINDING; PROTEIN DEGRADATION; STOICHIOMETRY; XENOPUS;

ANIMALS; DNA; DNA-BINDING PROTEINS; HISTONES; NUCLEOSOMES; RNA, RIBOSOMAL, 5S; TRANSCRIPTION FACTOR TFIIIA; TRANSCRIPTION FACTORS; XENOPUS;

XENOPUS BOREALIS;

EID: 0034002481     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.6.2167-2175.2000     Document Type: Article

References (62)

1. Allan, J., N. Harborne, D. C. Rau, and H. Gould. 1982. Participation of the core histone tails in the stabilization of the chromatin solenoid, J. Cell Biol. 93:285-297.
2. Andrews, M. T., and D. D. Brown. 1987. Transient activation of oocyte 5S RNA genes in Xenopus embryos by raising the level of the trans-acting factor TFIIIA. Cell 51:445-453.
3. Ausio, J., F. Dong, and K. E. van Holde. 1989. Use of selectively trypsinized nucleosome core particles to analyze the role of the histone 'tails' in the stabilization of the nucleosome. J. Mol. Biol. 206:451-463.
4. Bauer, W. R., J. J. Hayes, J. H. White, and A. P. Wolffe. 1994. Nucleosome structural changes due to acetylation. J. Mol. Biol. 236:685-690.
5. Bohm, L., G. Briand, P. Sautiere, and C. Crane-Robinson. 1982. Proteolytic digestion studies of chromatin core-histone structure. Identification of limit peptides from histone H2B. Eur. J. Biochem. 123:299-303.
6. Bouvet, P., S. Dimitrov, and A. P. Wolffe. 1994. Specific regulation of chromosomal 5S rRNA gene transcription in vivo by histone H1. Genes Dev. 8:1147-1159.
7. Brownell, J. E., and C. D. Allis. 1996. Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation. Curr. Opin. Genet. Dev. 6:175-184.
8. Cary, P. D., C. Crane-Robinson, E. M. Bradbury, and G. H. Dixon. 1982. Effect of acetylation on the binding of N-terminal peptides of histone H4 to DNA. Eur. J. Biochem. 127:137-143.
9. Clark, D. J., and A. P. Wolffe. 1991. Superhelical stress and nucleosome-mediated repression of 5S RNA gene transcription in vitro. EMBO J. 10: 3419-3428.
10. Del Rio, S., and D. R. Setzer. 1991. High yield purification of active transcription factor IIIA expressed in E. coli. Nucleic Acids Res. 19:6197-6203.
11. Felsenfeld, G. 1992. Chromatin as an essential part of the transcriptional mechanism. Nature 355:219-224.
12. Flaus, A., K. Luger, S. Tan, and T. J. Richmond. 1996. Mapping nucleosome position at single base-pair resolution by using site-directed hydroxyl radicals. Proc. Natl. Acad. Sci. USA 93:1370-1375.
13. Garcia-Ramirez, M., F. Dong, and J. Ausio. 1992. Role of the histone 'tails' in the folding of oligonucleosomes depleted of histone H1. J. Biol. Chem. 267:19587-19595.
14. Garcia-Ramirez, M., C. Rocchini, and J. Ausio. 1995. Modulation of chromatin folding by histone acetylation. J. Biol. Chem. 270:17923-17928.
15. Godde, J. S., Y. Nakatani, and A. P. Wolffe. 1995. The amino-terminal tails of the core histones and the translational position of the TATA box determine TBP/TFIIA association with nucleosomal DNA. Nucleic Acids Res. 23:4557-4564.
16. Gottesfeld, J. M., and L. S. Bloomer. 1982. Assembly of transcriptionally active 5S RNA gene chromatin in vitro. Cell 28:781-791.
17. Grunstein, M. 1992. Histones as regulators of genes. Sci. Am. 267:68-74.
18. Hamiche, A., R. Sandaltzopoulos, D. A. Gdula, and C. Wu. 1999. ATP-dependent histone octamer sliding mediated by the chromatin remodeling complex NURF. Cell 97:833-842.
19. Hansen, J. 1997. The core histone amino termini: combinatorial interaction domains that link chromatin structure with function. Chemtracts Biochem. Mol. Biol. 10:737-750.
20. Hansen, J. C., C. Tse, and A. P. Wolffe. 1998. Structure and function of the core histone N-termini: more than meets the eye. Biochemistry 37:17637-17641.
21. Hansen, J. C., and A. P. Wolffe. 1994. A role for histones H2A/H2B in chromatin folding and transcriptional repression. Proc. Natl. Acad. Sci. USA 91:2339-2343.
22. Hayes, J. J., D. Clark, and A. P. Wolffe. 1991. Histone contributions to the structure of DNA in the nucleosome. Proc. Natl. Acad. Sci. USA 88:6829-6833.
23. Hayes, J. J., D. Pruss, and A. P. Wolffe. 1994. Contacts of the globular domain of histone H5 and core histones with DNA in a 'chromatosome'. Proc. Natl. Acad. Sci. USA 91:7817-7821.
24. Hayes, J. J., T. D. Tullius, and A. P. Wolffe. 1990. The structure of DNA in a nucleosome. Proc. Natl. Acad. Sci. USA 87:7405-7409.
25. Hayes, J. J., and A. P. Wolffe. 1992. Histones H2A/H2B inhibit the interaction of TFIIIA with a nucleosome including the Xenopus borealis somatic 5S RNA gene. Proc. Natl. Acad. Sci. USA 89:1229-1233.
26. Howe, L., and J. Ausio. 1998. Nucleosome translational position, not histone acetylation, determines TFIIIA binding to nucleosomal Xenopus laevis 5S rRNA genes. Mol. Cell. Biol. 18:1156-1162.
27. Howe, L., T. A. Ranalli, C. D. Allis, and J. Ausio. 1998. Transcriptionally active Xenopus laevis somatic 5 S ribosomal RNA genes are packaged with hyperacetylated histone H4, whereas transcriptionally silent oocyte genes are not. J. Biol. Chem. 273:20693-20696.
28. Kuo, M. H., and C. D. Allis. 1998. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20:615-626.
29. Lassar, A. B., P. L. Martin, and R. G. Roeder. 1983. Transcription of class III genes: formation of preinitiation complexes. Science 222:740-748.
30. Lee, D., J. J. Hayes, D. Pruss, and A. P. Wolffe. 1993. A positive role for histone acetylation in transcription factor binding to nucleosomal DNA. Cell 72:73-84.
31. Lee, K.-M., and J. J. Hayes. 1997. The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core. Proc. Natl. Acad. Sci. USA 94:8959-8964.
32. Lee, K. M., and J. J. Hayes. 1998. Linker DNA and H1-dependent reorganization of histone-DNA interactions within the nucleosome. Biochemistry 37:8622-8628.
33. 2 termini. J. Biol. Chem. 273:12288-12295.
34. Luger, K., A. W. Mader, R. K. Richmond, D. F. Sargent, and T. J. Richmond. 1997. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389:251-260.
35. Norton, V. G., B. S. Imai, P. Van, and E. M. Bradbury. 1989. Histone acetylation reduces nucleosome core particle linking number change. Cell 57:449-457.
36. Norton, V. G., K. W. Marvin, P. Yau, and E. M. Bradbury. 1990. Nucleosome linking number change controlled by acetylation of histones H3 and H4. J. Mol. Biol. 265:19848-19852.
37. Panetta, G., M. Buttinelli, A. Flaus, T. J. Richmond, and D. Rhodes. 1998. Differential nucleosome positioning on Xenopus oocyte and somatic 5S RNA genes determines both TFIIIA and H1 binding: a mechanism for selective H1 repression. J. Mol. Biol. 282:683-697.
38. Pennings, S., G. Meersseman, and E. M. Bradbury. 1994. Linker histones H1 and H5 prevent the mobility of positioned nucleosomes. Proc. Natl. Acad. Sci. USA 91:10275-10279.
39. Polach, K. J., and J. Widom. 1995. Mechanism of protein access to specific DNA sequences in chromatin: a dynamic equilibrium model for gene regulation. J. Mol. Biol. 254:130-149.
40. Polach, K. J., and J. Widom. 1996. A model for the cooperative binding of eukaryotic regulatory proteins to nucleosomal target sites. J. Mol. Biol. 258:800-812.
41. Pruss, D., and A. P. Wolffe. 1993. Histone-DNA contacts in a nucleosome core containing a Xenopus 5S rRNA gene. Biochemistry 32:6810-6814.
42. Rhodes, D. 1985. Structural analysis of a triple complex between the histone octamer, a Xenopus gene for 5S RNA and transcription factor IIIA. EMBO J. 4:3473-3482.
43. Sakonju, S., and D. D. Brown. 1982. Contact points between a positive transcription factor and the Xenopus 5S RNA gene. Cell 31:395-405.
44. Schwartz, P. M., and J. C. Hansen. 1994. Formation and stability of higher order chromatin structures. J. Biol. Chem. 269:16284-16289.
45. Sera, T., and A. P. Wolffe. 1998. Role of histone H1 as an architectural determinant of chromatin structure and as a specific repressor of transcription on Xenopus oocyte 5S rRNA genes. Mol. Cell. Biol. 18:3668-3680.
46. Simpson, R. T. 1990. Nucleosome positioning can affect the function of a cis-acting DNA element in vivo. Nature 343:387-389.
47. Smith, D. R., I. J. Jackson, and D. D. Brown. 1984. Domains of the positive transcription factor specific for the Xenopus 5S RNA gene. Cell 37:645-652.
48. Straka, C., and W. A. Horz. 1991. Functional role for nucleosomes in the repression of a yeast promoter. EMBO J. 10:361-368.
49. Thiriet, C., and P. Albert. 1995. Rapid and effective Western blotting of histones from acid-urea-Triton and sodium dodecyl sulfate polyacrylamide gels: two different approaches depending on the subsequent qualitative or quantitative analysis. Electrophoresis 16:357-361.
50. Thiriet, C., and J. J. Hayes. 1997. Antisera directed against anti-histone H4 antibodies recognize linker histones. Novel immunological probes to detect histone interactions. J. Biol. Chem. 272:18740-18745.
51. Thiriet, C., and J. J. Hayes. 1998. Functionally relevant histone-DNA interactions extend beyond the classically defined nucleosome core region. J. Biol. Chem. 273:21352-21358.
52. Tomaszewski, R., E. Mogielnicka, and A. Jerzmanowski. 1998. Both the 5S rRNA gene and the AT-rich flanks of Xenopus laevis oocyte-type 5S rDNA repeat are required for histone H1-dependent repression of transcription of pol III-type genes in in vitro reconstituted chromatin. Nucleic Acids Res. 26:5596-5601.
53. Tremethick, D., K. Zucker, and A. Worcel. 1990. The transcription complex of the 5S RNA gene, but not transcription factor TFIIIA alone, prevents nucleosomal repression of transcription. J. Biol. Chem. 265:5014-5023.
54. Tse, C., T. M. Fletcher, and J. C. Hansen. 1998. Enhanced transcription factor access to arrays of histone H3/H4 tetramer. DNA complexes in vitro: implications for replication and transcription. Proc. Natl. Acad. Sci. USA 95:12169-12173.
55. Tse, C., T. Sera, A. P. Wolffe, and J. C. Hansen. 1998. Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III. Mol. Cell. Biol. 18:4629-4638.
56. Ura, K., J. J. Hayes, and A. P. Wolffe. 1995. A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: restriction by linker histones. EMBO J. 14:3752-3765.
57. Vettese-Dadey, M., P. A. Grant, T. R. Hebbes, C. Crane-Robinson, C. D. Allis, and J. L. Workman. 1996. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J. 15:2508-2518.
58. Vettese-Dadey, M., P. Walter, H. Chen, L.-J. Juan, and J. L. Workman. 1994. Role of the histone amino termini in facilitated binding of a transcription factor, GAL4-AH, to nucleosome cores. Mol. Cell. Biol. 14:970-981.
59. Wolffe, A. P. 1998. Chromatin: structure and function. Academic Press, London, England.
60. Wolffe, A. P., and D. D. Brown. 1988. Developmental regulation of two 5S ribosomal RNA genes. Science 241:1626-1632.
61. Wolffe, A. P., and J. J. Hayes. 1999. Chromatin disruption and modification. Nucleic Acids Res. 27:711-720.
62. Wolffe, A. P., and J. J. Hayes. 1993. Transcription factor interactions with model nucleosomal templates. Methods Mol. Genet. 2:314-330.