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. 1995 Dec 5;92(25):11328–11330. doi: 10.1073/pnas.92.25.11328

The histone fold: evolutionary questions.

V Ramakrishnan 1
PMCID: PMC40393  PMID: 8524779

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arents G., Burlingame R. W., Wang B. C., Love W. E., Moudrianakis E. N. The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10148–10152. doi: 10.1073/pnas.88.22.10148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Arents G., Moudrianakis E. N. The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):11170–11174. doi: 10.1073/pnas.92.24.11170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Arents G., Moudrianakis E. N. Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10489–10493. doi: 10.1073/pnas.90.22.10489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Baer B. W., Rhodes D. Eukaryotic RNA polymerase II binds to nucleosome cores from transcribed genes. Nature. 1983 Feb 10;301(5900):482–488. doi: 10.1038/301482a0. [DOI] [PubMed] [Google Scholar]
  5. Baxevanis A. D., Arents G., Moudrianakis E. N., Landsman D. A variety of DNA-binding and multimeric proteins contain the histone fold motif. Nucleic Acids Res. 1995 Jul 25;23(14):2685–2691. doi: 10.1093/nar/23.14.2685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Brown A. P. Codon-level analysis of histone primary sequence: evidence of a repeat tetrapeptide origin and later inclusion of transcribed sequence. J Theor Biol. 1983 Oct 7;104(3):401–416. doi: 10.1016/0022-5193(83)90114-5. [DOI] [PubMed] [Google Scholar]
  7. Böhm L., Hayashi H., Cary P. D., Moss T., Crane-Robinson C., Bradbury E. M. Sites of histone/histone interaction in the H3 - H4 complex. Eur J Biochem. 1977 Aug 1;77(3):487–493. doi: 10.1111/j.1432-1033.1977.tb11690.x. [DOI] [PubMed] [Google Scholar]
  8. Cerf C., Lippens G., Ramakrishnan V., Muyldermans S., Segers A., Wyns L., Wodak S. J., 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. 1994 Sep 20;33(37):11079–11086. doi: 10.1021/bi00203a004. [DOI] [PubMed] [Google Scholar]
  9. Clark K. L., Halay E. D., Lai E., Burley S. K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature. 1993 Jul 29;364(6436):412–420. doi: 10.1038/364412a0. [DOI] [PubMed] [Google Scholar]
  10. D'Anna J. A., Jr, Isenberg I. A histone cross-complexing pattern. Biochemistry. 1974 Nov 19;13(24):4992–4997. doi: 10.1021/bi00721a019. [DOI] [PubMed] [Google Scholar]
  11. Dong F., van Holde K. E. Nucleosome positioning is determined by the (H3-H4)2 tetramer. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10596–10600. doi: 10.1073/pnas.88.23.10596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Griffith J. D. Visualization of prokaryotic DNA in a regularly condensed chromatin-like fiber. Proc Natl Acad Sci U S A. 1976 Feb;73(2):563–567. doi: 10.1073/pnas.73.2.563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hayes J. J., Clark D. J., Wolffe A. P. Histone contributions to the structure of DNA in the nucleosome. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6829–6833. doi: 10.1073/pnas.88.15.6829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hayes J. J., Wolffe A. P. Histones H2A/H2B inhibit the interaction of transcription factor IIIA with the Xenopus borealis somatic 5S RNA gene in a nucleosome. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1229–1233. doi: 10.1073/pnas.89.4.1229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Klug A., Rhodes D., Smith J., Finch J. T., Thomas J. O. A low resolution structure for the histone core of the nucleosome. Nature. 1980 Oct 9;287(5782):509–516. doi: 10.1038/287509a0. [DOI] [PubMed] [Google Scholar]
  16. Kokubo T., Gong D. W., Wootton J. C., Horikoshi M., Roeder R. G., Nakatani Y. Molecular cloning of Drosophila TFIID subunits. Nature. 1994 Feb 3;367(6462):484–487. doi: 10.1038/367484a0. [DOI] [PubMed] [Google Scholar]
  17. Kornberg R. D. Chromatin structure: a repeating unit of histones and DNA. Science. 1974 May 24;184(4139):868–871. doi: 10.1126/science.184.4139.868. [DOI] [PubMed] [Google Scholar]
  18. Kornberg R. D., Thomas J. O. Chromatin structure; oligomers of the histones. Science. 1974 May 24;184(4139):865–868. doi: 10.1126/science.184.4139.865. [DOI] [PubMed] [Google Scholar]
  19. Moss T., Cary P. D., Abercrombie B. D., Crane-Robinson C., Bradbury E. M. A pH-dependent interaction between histones H2A and H2B involving secondary and tertiary folding. Eur J Biochem. 1976 Dec 11;71(2):337–350. doi: 10.1111/j.1432-1033.1976.tb11120.x. [DOI] [PubMed] [Google Scholar]
  20. Ramakrishnan V., Finch J. T., Graziano V., Lee P. L., Sweet R. M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature. 1993 Mar 18;362(6417):219–223. doi: 10.1038/362219a0. [DOI] [PubMed] [Google Scholar]
  21. Reeck G. R., Swanson E., Teller D. C. The evolution of histones. J Mol Evol. 1978 Feb 21;10(4):309–317. doi: 10.1007/BF01734220. [DOI] [PubMed] [Google Scholar]
  22. Richmond T. J., Finch J. T., Rushton B., Rhodes D., Klug A. Structure of the nucleosome core particle at 7 A resolution. Nature. 1984 Oct 11;311(5986):532–537. doi: 10.1038/311532a0. [DOI] [PubMed] [Google Scholar]
  23. Stoler S., Keith K. C., Curnick K. E., Fitzgerald-Hayes M. A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis. Genes Dev. 1995 Mar 1;9(5):573–586. doi: 10.1101/gad.9.5.573. [DOI] [PubMed] [Google Scholar]
  24. Sullivan K. F., Hechenberger M., Masri K. Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere. J Cell Biol. 1994 Nov;127(3):581–592. doi: 10.1083/jcb.127.3.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Tanaka I., Appelt K., Dijk J., White S. W., Wilson K. S. 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature. 1984 Aug 2;310(5976):376–381. doi: 10.1038/310376a0. [DOI] [PubMed] [Google Scholar]
  26. Thatcher T. H., Gorovsky M. A. Phylogenetic analysis of the core histones H2A, H2B, H3, and H4. Nucleic Acids Res. 1994 Jan 25;22(2):174–179. doi: 10.1093/nar/22.2.174. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Wells D., Brown D. Histone and histone gene compilation and alignment update. Nucleic Acids Res. 1991 Apr 25;19 (Suppl):2173–2188. doi: 10.1093/nar/19.suppl.2173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wells D., McBride C. A comprehensive compilation and alignment of histones and histone genes. Nucleic Acids Res. 1989;17 (Suppl):r311–r346. doi: 10.1093/nar/17.suppl.r311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Wuilmart C., Wyns L. An evolutionaty scheme for the histones as derived from a study of internal repetitions and homologies among the different classes. J Theor Biol. 1977 Mar 21;65(2):231–252. doi: 10.1016/0022-5193(77)90323-x. [DOI] [PubMed] [Google Scholar]

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