The role of histone H1 in chromatin condensation and transcriptional repression

Genetica

Volumn 106, Issue 1-2, 1999, Pages 117-124

  Buttinelli, Memmo ^a,b   Panetta, Gianna ^b   Rhodes, Daniela ^b   Travers, Andrew ^b  

^a CNR   (Italy)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

Chromatin condensation; H1 transcriptional repression; H5 location; Linker histories; Nucleosome positioning

Indexed keywords

AMPHIBIA; ANIMALIA; REPTILIA; XENOPUS BOREALIS;

EID: 0033400839     PISSN: 00166707     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1003745315540     Document Type: Article

References (59)

1. Travers A. (1999) Towards a higher order structure for chromatin - the location of the linker histone in the nucleosome. Trends Biochem. Sci. 24 (1999): 4-7.
2. Simpson R.T.: Structure of the chromatosome, a chromatin particle containing 160 bp of DNA and all histones. Biochemistry 17 (1978): 5524-5531.
3. Graziano V., Gerchmann S.E., Schneider D.K. and Ramakrishnan V.: Histone H1 is located in the interior of the chromatin 30-nm filament. Nature 368 (1994): 351-354.
4. Crane-Robinson C.: Where is the globular domain of linker histone located on the nucleosome? Trends Biochem. Sci. 22 (1997): 75-77.
5. Thoma F., Köller T. and Klug A.: Involvement of histone H1 in the organization of the nucleosome and of the salt dependent superstructure of chromatin. J. Cell Biol. 83 (1979): 403.
6. Bednar J., Horowitz R.A., Dubochet J. and Woodcock C.L.: Chromatin conformation and salt-induced compaction: three-dimensional structural information from cryoelectron microscopy. J. Cell Biol. 131 (1995): 1365-1376.
7. Ramakrishnan V., Finch J.T., Graziano V., Lee P.L. and Sweet R.M.: Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding. Nature 362 (1993): 219-223.
8. Cerf C., Lippens G., Ramakrishnan V., Muyldermans S., Segers A., Wyns L., Wodak S.J. and Hallenga K.: 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 histone H5. Biochemistry 33 (1994): 11079-11086.
9. Thomas J.O., Rees C. and Finch J.T.: Cooperative binding of the globular domains of histones H1 and H5 to DNA Nucl. Acids. Res. 20 (1992): 187-194.
10. Draves P.H., Lowary P.T. and Widom J.: Cooperative binding of the globular domain of histone H5 to DNA. J. Mol. Biol.225 (1992): 1105-1121.
11. Goytisolo F.A. Gerchman S.E., Yu X., Rees C., Graziano V., Ramakrishnan V. and Thomas J.O.: Identification of two DNA-binding sites on the globular domain of histone H5. EMBO J. 15 (1996): 3421-3429.
12. Zhou Y.-B., Gerchman S.E., Ramakrishnan V., Travers A. and Muyldermans S.: Position and orientation of the globular domain of linker histone H5 on the nucleosome. Nature 395 (1998): 402-405.
13. Thomas J.O. and Wilson C.M.: Selective radiolabeling and identification of a strong nucleosome binding site on the globular domain of histone H5. EMBO J. 5 (1986): 3531-3537.
14. An W., Leuba S.H., van Holde K. and Zlatanova J.: Linker histone protects DNA on only one side of the core particle, in a sequence-dependent manner. Proc. Natl. Acad. Sci. USA, 95 (1998): 3396-3401.
15. Wong J., Li Q., Levi B.-Z., Shi Y.-B. and Wolffe A.P.: Structural and functional features of a specific nucleosome containing a recognition element for the thyroid hormone receptor. EMBO J. 17 (1998): 520-534.
16. Satchwell S.C. and Travers A.A.: Asymmetry and polarity of nucleosomes in chicken erythrocyte chromatin. EMBO J. 8 (1989): 229-238.
17. Muyldermans S.V. and Travers A.A.: DNA sequence organization in chromatosomes. J. Mol. Biol. 235 (1994): 855-870.
18. Travers A.A. and Muyldermans S.V.: A DNA sequence for positioning chromatosomes. J. Mol. Biol. 257 (1996): 486-491.
19. Allan J., Crane-Robinson C. and Aviles F.X.: The structure of histone H1 and its location in chromatin. Nature 288 (1980): 675-679.
20. Pruss D., Bartholomew B., Persinger J., Hayes J., Arents G., Moudrianakis M.N. and Wolffe A.P.: An asymmetric model for the nucleosome: A binding site for linker histones inside the DNA gyres. Science 274 (1996): 614-617.
21. Hayes J.J.: Site-directed cleavage of DNA by a linker histone-Fe(II) EDTA conjugate: Localization of a globular domain binding site within a nucleosome. Biochemistry 35 (1996): 11931-11937.
22. Hayes J.J., and Wolffe A.P.: Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome. Proc. Natl. Acad. Sci. USA 90 (1993): 6415-6419.
23. Hamiche A., Schultz P., Ramakrishnan V., Oudet P. and Prunell A.: Linker histone dependent DNA structure in mononucleosomes. J. Mol. Biol. 257 (1996): 30-42.
24. Lee K.M. and Hayes J.J.: Linker DNA and H1-dependent reorganization of histone-DNA interactions within the nucleosome. Biochemistry 37 (1998): 8622-8628.
25. An W., van Holde K. and Zlatanova J.: Linker histone protection of chromatosomes reconstituted on 5S rDNA from Xenopus borealis: a reinvestigation. Nucl. Acids Res. 26 (1998): 4042-4047.
26. Panetta G., Buttinelli M., Flaus A., Richmond T.J. and Rhodes D.: 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 (1998): 683-697.
27. Flaus A., Luger K., Tan S. and Richmond T.J.: Mapping nucleosome position at single base-pair resolution by using site-directed hydroxyl radicals. Proc. Natl. Acad. Sci. USA, 93 (1996): 1370-1375.
28. Drew H.R. and Calladine C.R.: Sequence-specific positioning of core histones on an 860 base-pair DNA. Experiment and theory. J. Mol. Biol., 195 (1987): 143-173.
29. Dong F., Hansen J.C. and van Holde K.E.: DNA and protein determinants of nucleosome positioning on sea urchin 5Sr-RNA gene sequences in vitro. Proc. Natl. Acad. Sci. USA, 87 (1990): 5724-5728.
30. Pruss D. and Wolffe A.P.: Histone-DNA contacts in a nucleosome core containing a 5S rRNA gene. Biochemistry 32 (1993): 6810-6814.
31. Sera T. and Wolffe A.P.: 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 (1998): 3668-3680.
32. Howe L. and Ausió J.: Nucleosome translational position, not histone acetylation, determines TFIIIA binding to nucleosomal Xenopus laevis 5S rRNA genes. Mol. Cell. Biol. 18 (1998): 1156-1162.
33. Kruger W., Peterson C.L., Sil A., Coburn C., Arents G., Moudrianakis E.N. and Herskowitz I.: Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription. Genes. Dev. 9 (1995): 2770-2779.
34. Luger K., Mäder A.W., Richmond R.K., Sargent D. L. and Richmond T.J.: Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389 (1997): 251-260.
35. Luger K., Rechesteiner T.J., Flaus A.J, Waye M.M and Richmond T.J.: Characterization of nucleosome core particles containing histone proteins made in bacteria. J. Mol. Biol. 272 (1997): 301-311
36. Buttinelli M., Di Mauro E. and Negri R.: Multiple nucleosome positioning with unique rotational setting for the Saccharomyces cerevisiae 5S rRNA gene in vitro and in vivo. Proc. Natl. Acad. Sci. USA, 90 (1993): 9315-9319.
37. Laybourn P.J. and Kadonaga J.T.: Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II. Science, 254 (1991): 238-245.
38. Juan L.J., Utley R.T., Vignali M., Bohm L. and Workman J.L.: H1-mediated repression of transcription factor binding to a stably positioned nucleosome. J. Biol. Chem. 272 (1997): 3635-3640.
39. Wormington W.M. and Brown D.D.: Onset of 5S RNA gene regulation during Xenopus embryogenesis. Dev. Biol., 99 (1983): 248-257.
40. Peterson R.C., Doering J.L. and Brown D.D.: Characterization of two Xenopus somatic 5S DNAs and one minor oocyte-specific 5S DNA. Cell 20 (1980): 131-141.
41. Engelke D.R., Ng S.Y., Shastry B.S. and Roeder R.G.: Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes. Cell 19 (1980): 717-728.
42. McConkey G.A. and Bogenhagen D.E.: TFIIIA binds with equal affinity to somatic and major oocyte 5S RNA genes. Genes Dev. 2 (1988): 205-214.
43. Schlissel M.S. and Brown D.D.: The transcriptional regulation of Xenopus 5S RNA genes in chromatin: the roles of active stable transcription complexes and histone H1. Cell 37 (1984): 903-913.
44. Wolffe A.P. and Brown D.D.: Developmental regulation of two 5S ribosomal RNA genes. Science 241 (1988): 1626-1632.
45. Seidel C.W. and Peck L.J.: Kinetic control of 5S RNA gene transcription. J. Mol. Biol. 227 (1992): 1009-1018.
46. Pelham H.R., Wormington W.M. and Brown D.D.: Related 5S RNA transcription factors in Xenopus oocytes and somatic cells. Proc. Natl. Acad. Sci. USA, 78 (1981): 1760-1764.
47. Shastry B.S., Honda B.M. and Roeder R.G.: Altered levels of a 5S gene-specific transcription factor (TFIIIA) during oogenesis and embryonic development of Xenopus laevis. J. Biol. Chem. 259 (1984): 11373-11382.
48. Bouvet P., Dimitrov S. and Wolffe A.P.: Specific regulation of Xenopus chromosomal 5S rRNA gene transcription in vivo by histone H1. Genes Dev. 8 (1994): 1147-1159.
49. Kandolf H.: The H1A histone variant is an in vivo repressor of oocyte-type 5S gene transcription in Xenopus laevis embryos. Proc. Natl. Acad. Sci. USA, 91 (1994): 7257-7261.
50. Flynn J.M. and Woodland H.R.: The synthesis of histone H1 during early amphibian development. Dev. Biol. 75 (1980): 222-230.
51. Korn L.J. and Gurdon J.B.: The reactivation of developmentally inert 5S genes in somatic nuclei injected into Xenopus oocytes. Nature, 289 (1981): 461-465.
52. Gottesfeld J.M. and Bloomer L.S.: Nonrandom alignment of nucleosomes on 5S RNA genes of X. laevis. Cell 21 (1980): 751-760.
53. Young D. and Carroll D.: Regular arrangement of nucleosomes on 5S rRNA genes in Xenopus laevis. Mol. Cell. Biol. 3 (1983): 720-730.
54. Chipev C.C. and Wolffe A.P.: Chromosomal organization of Xenopus laevis oocyte and somatic 5S rRNA genes in vivo. Mol. Cell. Biol. 12 (1992): 45-55.
55. Rhodes D.: Structural analysis of a triple complex between the histone octamer, a Xenopus gene for 5S RNA and transcription factor IIIA. EMBO J. 4 (1985): 3473-3482.
56. Finch J.T. and Klug A.: Solenoidal model for superstructure in chromatin. Proc. Natl. Acad. Sci. USA, 73 (1976): 1897-1901.
57. Korn L.J. and Brown D.D.: Nucleotide sequence of Xenopus borealis oocyte 5S DNA: comparison of sequences that flank several related eucaryotic genes. Cell, 15 (1978): 1145-1156.
58. Tomaszewski R. and Jerzmanowski A.: The AT-rich flanks of the oocyte-type 5S RNA gene of Xenopus laevis act as a strong local signal for histone H1-mediated chromatin reorganization in vitro. Nucl. Acids Res. 25 (1997): 458-466.
59. Vignali M. and Workman J.L.: Location and function of linker histones. Nature Struc. Biol. 5 (1998): 1025-1028.