Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1998 Jun 15;26(12):2837–2842. doi: 10.1093/nar/26.12.2837

Evolutionary conservation of histone macroH2A subtypes and domains.

J R Pehrson 1, R N Fuji 1
PMCID: PMC147630  PMID: 9611225

Abstract

Histone macroH2A is an unusual core histone that contains a large non-histone region, and a region that resembles a full length H2A. We examined theconservation of this novel structural arrangement by cloning chicken macroH2A cDNAs and comparing them to their rat counterparts. The amino acid sequences of the two known macroH2A subtypes are >95% identical between these species despite evolutionary separation of approximately 300 million years. The H2A region of macroH2A is completely conserved, and thus is even more conserved than conventional H2A in these species. The origin of the non-histone domain was examined by comparing its sequence to proteins found in bacteria and RNA viruses. These comparisons indicate that this domain is derived from a gene that originated prior to the appearance of eukaryotes, and suggest that the non-histone region has retained the basic function of its ancestral gene.

Full Text

The Full Text of this article is available as a PDF (144.1 KB).

Selected References

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

  1. Baxevanis A. D., Landsman D. Histone and histone fold sequences and structures: a database. Nucleic Acids Res. 1997 Jan 1;25(1):272–273. doi: 10.1093/nar/25.1.272. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bruns G. A., Ingram V. M. The erythroid cells and haemoglobins of the chick embryo. Philos Trans R Soc Lond B Biol Sci. 1973 Oct 25;266(877):225–305. doi: 10.1098/rstb.1973.0050. [DOI] [PubMed] [Google Scholar]
  3. Dominguez G., Wang C. Y., Frey T. K. Sequence of the genome RNA of rubella virus: evidence for genetic rearrangement during togavirus evolution. Virology. 1990 Jul;177(1):225–238. doi: 10.1016/0042-6822(90)90476-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Doolittle R. F., Feng D. F., Tsang S., Cho G., Little E. Determining divergence times of the major kingdoms of living organisms with a protein clock. Science. 1996 Jan 26;271(5248):470–477. doi: 10.1126/science.271.5248.470. [DOI] [PubMed] [Google Scholar]
  5. Earnshaw W. C., Rothfield N. Identification of a family of human centromere proteins using autoimmune sera from patients with scleroderma. Chromosoma. 1985;91(3-4):313–321. doi: 10.1007/BF00328227. [DOI] [PubMed] [Google Scholar]
  6. Gassmann M., Thömmes P., Weiser T., Hübscher U. Efficient production of chicken egg yolk antibodies against a conserved mammalian protein. FASEB J. 1990 May;4(8):2528–2532. doi: 10.1096/fasebj.4.8.1970792. [DOI] [PubMed] [Google Scholar]
  7. Gorbalenya A. E., Koonin E. V., Lai M. M. Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi- and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses. FEBS Lett. 1991 Aug 19;288(1-2):201–205. doi: 10.1016/0014-5793(91)81034-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hatch C. L., Bonner W. M. Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but highly conserved basal histone H2A isoprotein species. Nucleic Acids Res. 1988 Feb 11;16(3):1113–1124. doi: 10.1093/nar/16.3.1113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kaelin W. G., Jr, Pallas D. C., DeCaprio J. A., Kaye F. J., Livingston D. M. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product. Cell. 1991 Feb 8;64(3):521–532. doi: 10.1016/0092-8674(91)90236-r. [DOI] [PubMed] [Google Scholar]
  10. Kirchgessner T. G., Heinzmann C., Svenson K. L., Gordon D. A., Nicosia M., Lebherz H. G., Lusis A. J., Williams D. L. Regulation of chicken apolipoprotein B: cloning, tissue distribution, and estrogen induction of mRNA. Gene. 1987;59(2-3):241–251. doi: 10.1016/0378-1119(87)90332-5. [DOI] [PubMed] [Google Scholar]
  11. LaStarza M. W., Lemm J. A., Rice C. M. Genetic analysis of the nsP3 region of Sindbis virus: evidence for roles in minus-strand and subgenomic RNA synthesis. J Virol. 1994 Sep;68(9):5781–5791. doi: 10.1128/jvi.68.9.5781-5791.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Liu X., Li B., GorovskyMA Essential and nonessential histone H2A variants in Tetrahymena thermophila. Mol Cell Biol. 1996 Aug;16(8):4305–4311. doi: 10.1128/mcb.16.8.4305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Page R. D. TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosci. 1996 Aug;12(4):357–358. doi: 10.1093/bioinformatics/12.4.357. [DOI] [PubMed] [Google Scholar]
  14. Palmer D. K., O'Day K., Trong H. L., Charbonneau H., Margolis R. L. Purification of the centromere-specific protein CENP-A and demonstration that it is a distinctive histone. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3734–3738. doi: 10.1073/pnas.88.9.3734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Palmer D. K., O'Day K., Wener M. H., Andrews B. S., Margolis R. L. A 17-kD centromere protein (CENP-A) copurifies with nucleosome core particles and with histones. J Cell Biol. 1987 Apr;104(4):805–815. doi: 10.1083/jcb.104.4.805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pehrson J. R., Costanzi C., Dharia C. Developmental and tissue expression patterns of histone macroH2A1 subtypes. J Cell Biochem. 1997 Apr;65(1):107–113. doi: 10.1002/(sici)1097-4644(199704)65:1<107::aid-jcb11>3.0.co;2-h. [DOI] [PubMed] [Google Scholar]
  17. Pehrson J. R., Fried V. A. MacroH2A, a core histone containing a large nonhistone region. Science. 1992 Sep 4;257(5075):1398–1400. doi: 10.1126/science.1529340. [DOI] [PubMed] [Google Scholar]
  18. Pehrson J. R. Thymine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9149–9153. doi: 10.1073/pnas.86.23.9149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988 Jul 15;67(1):31–40. doi: 10.1016/0378-1119(88)90005-4. [DOI] [PubMed] [Google Scholar]
  21. 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]
  22. 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]
  23. Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994 Nov 11;22(22):4673–4680. doi: 10.1093/nar/22.22.4673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Valentin H. E., Zwingmann G., Schönebaum A., Steinbüchel A. Metabolic pathway for biosynthesis of poly(3-hydroxybutyrate-co-4-hydroxybutyrate) from 4-hydroxybutyrate by Alcaligenes eutrophus. Eur J Biochem. 1995 Jan 15;227(1-2):43–60. doi: 10.1111/j.1432-1033.1995.tb20358.x. [DOI] [PubMed] [Google Scholar]
  25. Wang Y. F., Sawicki S. G., Sawicki D. L. Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA. J Virol. 1994 Oct;68(10):6466–6475. doi: 10.1128/jvi.68.10.6466-6475.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Willard H. F., Salz H. K. Remodelling chromatin with RNA. Nature. 1997 Mar 20;386(6622):228–229. doi: 10.1038/386228a0. [DOI] [PubMed] [Google Scholar]
  27. van Daal A., Elgin S. C. A histone variant, H2AvD, is essential in Drosophila melanogaster. Mol Biol Cell. 1992 Jun;3(6):593–602. doi: 10.1091/mbc.3.6.593. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES