The role of histone H1 in chromatin condensation and transcriptional repression (original) (raw)

• 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.
  PubMed Google Scholar
• Simpson R.T.: Structure of the chromatosome, a chromatin particle containing 160 bp of DNA and all histones. Biochemistry 17 (1978): 5524–5531.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Crane-Robinson C.: Where is the globular domain of linker histone located on the nucleosome? Trends Biochem. Sci. 22 (1997): 75–77.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Satchwell S.C. and Travers A.A.: Asymmetry and polarity of nucleosomes in chicken erythrocyte chromatin. EMBO J. 8 (1989): 229–238.
  PubMed Google Scholar
• Muyldermans S.V. and Travers A.A.: DNA sequence organization in chromatosomes. J. Mol. Biol. 235 (1994): 855–870.
  PubMed Google Scholar
• Travers A.A. and Muyldermans S.V.: A DNA sequence for positioning chromatosomes. J. Mol. Biol. 257 (1996): 486–491.
  PubMed Google Scholar
• Allan J., Crane-Robinson C. and Aviles F.X.: The structure of histone H1 and its location in chromatin. Nature 288 (1980): 675–679.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Hamiche A., Schultz P., Ramakrishnan V., Oudet P. and Prunell A.: Linker histone dependent DNA structure in mono-nucleosomes. J. Mol. Biol. 257 (1996): 30–42.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Pruss D. and Wolffe A.P.: Histone-DNA contacts in a nucleosome core containing a 5S rRNA gene. Biochemistry 32 (1993): 6810–6814.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Wormington W.M. and Brown D.D.: Onset of 5S RNA gene regulation during Xenopus embryogenesis. Dev. Biol., 99 (1983): 248–257.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• McConkey G.A. and Bogenhagen D.F.: TFIIIA binds with equal affinity to somatic and major oocyte 5S RNA genes. Genes Dev. 2 (1988): 205–214.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Wolffe A.P. and Brown D.D.: Developmental regulation of two 5S ribosomal RNA genes. Science 241 (1988): 1626–1632.
  PubMed Google Scholar
• Seidel C.W. and Peck L.J.: Kinetic control of 5S RNA gene transcription. J. Mol. Biol. 227 (1992): 1009–1018.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Flynn J.M. and Woodland H.R.: The synthesis of histone H1 during early amphibian development. Dev. Biol. 75 (1980): 222–230.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Gottesfeld J.M. and Bloomer L.S.: Nonrandom alignment of nucleosomes on 5S RNA genes of X. laevis. Cell 21 (1980): 751–760.
  PubMed Google Scholar
• Young D. and Carroll D.: Regular arrangement of nucleosomes on 5S rRNA genes in Xenopus laevis. Mol. Cell. Biol. 3 (1983): 720–730.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Finch J.T. and Klug A.: Solenoidal model for superstructure in chromatin. Proc. Natl. Acad. Sci. USA, 73 (1976): 1897–1901.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• 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.
  PubMed Google Scholar
• Vignali M. and Workman J.L.: Location and function of linker histones. Nature Struc. Biol. 5 (1998): 1025–1028.
  Google Scholar