Czech J. Anim. Sci., 2015, 60(3):105-115 | DOI: 10.17221/8075-CJAS

A shift in erythrocyte histone H1 complement following selection in quail (Coturnix japonica)Original Paper

A. Kowalski1, J. Pa³yga1, S. Knaga2, A. Witkowski2
1 Department of Biochemistry and Genetics, Institute of Biology, Jan Kochanowski University, Kielce, Poland
2 Chair for Biological Bases of Animal Production, University of Life Sciences, Lublin, Poland

This work was aimed at comparing distribution of isoforms for polymorphic histone H1 variants H1.b and H1.z and variably abundant histone H1.d subtype between quail (Coturnix japonica) population selected for a high egg yolk cholesterol content and the control birds. The isoforms of histone H1.b (H1.b1, H1.b2) and histone H1.z (H1.z1, H1.z2) differed in their apparent molecular weights judging from their differential migration rates in one- and two-dimensional SDS-polyacrylamide gels. Stained histone H1.d bands and spots in one-dimensional acetic acid-urea and two-dimensional SDS-polyacrylamide gel patterns, respectively, exhibited differential intensities among quail individuals. Histone H1.d phenotypes with high (dh), intermediate (dhdl), and low (dl) amount of protein, displaying a small within-phenotype variability of the protein band intensities (coefficients of band variation below a threshold value of 0.25) were shown to be inherited in a Mendelian fashion with two alleles at a locus contributing to the band intensity. The frequencies of histone H1 alleles at loci H1.b2 = 13.32, d.f. = 1, P < 0.001), H1.z2 = 21.84, d.f. = 1, P < 0.001), and H1.d2 = 8.98, d.f. = 1, P < 0.01) were found to be statistically significant among the control and selected population. In general, a moderate degree of genetic divergence (FST equal to 0.07 and 0.1 at loci H1.b and H1.z, respectively) was observed among the control and selected quail populations. Selection may directly or indirectly affect the complement of H1 histones because of their presumably differential interactions with DNA and/or DNA-associated proteins resulting in alterations in the chromatin function.

Keywords: allelic variants; erythrocyte; histone H1 variants; phenotypic variants; quail; selection

Published: March 31, 2015  Show citation

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Kowalski A, Pa³yga J, Knaga S, Witkowski A. A shift in erythrocyte histone H1 complement following selection in quail (Coturnix japonica). Czech J. Anim. Sci. 2015;60(3):105-115. doi: 10.17221/8075-CJAS.
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References

  1. Baumgartner J., Koncekova Z., Benkova J. (2007): Line effect and phenotypic correlations among egg qualitative traits in Japanese quail eggs selected on yolk cholesterol content. Slovak Journal of Animal Science, 40, 13-18.
  2. Berdnikov V.A., Bogdanova V.S., Rozov S.M., Kosterin O.E. (1993): Geographic patterns of histone H1 allelic frequencies formed in the course of Pisum sativum L. (pea) cultivation. Heredity, 71, 199-209. Go to original source...
  3. Berdnikov V.A., Bogdanova V.S., Gorel F.L., Kosterin O.E., Trusov Y.A. (2003): Large changes in the structure of the major histone H1 subtype result in small effects on quantitative traits in legumes. Genetica, 119, 167-182. Go to original source... Go to PubMed...
  4. Bogdanova V.S., Lester D.R., Berdnikov V.A., Andersson I. (2005): Structure of allelic variants of subtype 5 of histone H1 in a pea Pisum sativum L. Heredity, 94, 582-588. Go to original source... Go to PubMed...
  5. Bogdanova V.S., Kosterin O.E., Berdnikov V.A. (2007): Phenotypic effect of substitution of allelic variants for a histone H1 subtype specific for growing tissues in the garden pea (Pisum sativum L.). Genetica, 130, 61-72. Go to original source... Go to PubMed...
  6. Bustin M., Catez F., Lim J.-H. (2005): The dynamics of histone H1 function in chromatin. Molecular Cell, 17, 617-620. Go to original source... Go to PubMed...
  7. Calvo S.E., Pagliarini D.J., Mootha V.K. (2009): Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans. Proceedings of the National Academy of Sciences the United States of America, 106, 7507-7512. Go to original source... Go to PubMed...
  8. Caterino T.L., Fang H., Hayes J.J. (2011): Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain. Molecular and Cellular Biology, 31, 2341-2348. Go to original source... Go to PubMed...
  9. Catez F., Ueda T., Bustin M. (2006): Determinants of histone H1 mobility and chromatin binding in living cells. Nature Structural and Molecular Biology, 13, 305-310. Go to original source... Go to PubMed...
  10. Clausell J., Happel N., Hale T.K., Doenecke D., Beato M. (2009): Histone H1 subtypes differently modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF. PLoS ONE, 4, e0007243. Go to original source... Go to PubMed...
  11. Dudnikov A.J. (2012): Geographic patterns of histone H1 encoding genes allelic variation in Aegilops tauschii Cos. (Poaceae). Molecular Biology Reports, 39, 2355-2363. Go to original source... Go to PubMed...
  12. Feuk L., Marshall C.L., Wintle R.F., Scherer S.W. (2006): Structural variants: changing the landscape of chromosomes and design of disease studies. Human Molecular Genetics, 15, 57-66. Go to original source... Go to PubMed...
  13. Furger A., Schurch N., Kurath U., Roditi I. (1997): Elements in the 3' untranslated region of procyclic mRNA regulate expresion in insect forms of Trypanosoma brucei by modulating RNA stability and translation. Molecular and Cellular Biology, 17, 4372-4380. Go to original source... Go to PubMed...
  14. Gornicka-Michalska E., Palyga J., Kowalski A., Cywa-Benko K. (2006): Sequence variants of chicken linker histone H1.a. FEBS Journal, 273, 1240-1250. Go to original source... Go to PubMed...
  15. Green A., Lonn A., Holmgren Peterson K., Ollinger K., Rundquist I. (2010): Translocation of histone H1 subtypes between chromatin and cytoplasm during mitosis in normal human fibroblasts. Cytometry Part A, 77, 478-484. Go to original source... Go to PubMed...
  16. Hansen J.C. (2002): Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms and function. Annual Review of Biophysical and Biomolecular Structure, 31, 361-392. Go to original source... Go to PubMed...
  17. Hansen J.C., Lu X., Ross E.D., Woody R.W. (2006): Intrinsic protein disorder, amino acid composition, and histone terminal domains. Journal of Biological Chemistry, 281, 1853-1856. Go to original source... Go to PubMed...
  18. Happel N., Doenecke D. (2009): Histone H1 and its isoforms: contribution to chromatin structure and function. Gene, 431, 1-12. Go to original source... Go to PubMed...
  19. Hashimoto H., Sonoda E., Takami Y., Kimura H., Nakayama T., Tachibana M., Takeda S., Shinkai Y. (2007): Histone H1 variant, H1R is involved in the DNA damage response. DNA Repair, 6, 1584-1595. Go to original source... Go to PubMed...
  20. Izzo A., Kamieniarz K., Schneider R. (2008): The histone H1 family: specific members, specific functions? Biological Chemistry, 389, 333-343. Go to original source... Go to PubMed...
  21. Kosterin O.E., Bogdanova V.S., Gorel F.L., Rozov S.M., Trusov Y.A., Berdnikov V.A. (1994): Histone H1 of the garden pea (Pisum sativum L.); composition, developmental changes, allelic polymorphism and inheritance. Plant Science, 101, 189-202. Go to original source...
  22. Kowalski A., Palyga J. (2012a): Linker histone subtypes and their allelic variants. Cell Biology International, 36, 981-996. Go to original source... Go to PubMed...
  23. Kowalski A., Palyga J. (2012b): High-resolution two-dimensional polyacrylamide gel electrophoresis: a tool for identification of polymorphic and modified linker histone components. In: Magdeldin S. (ed.): Gel Electrophoresis - Principles and Basics. InTech Croatia, Rijeka, Croatia, 117-136. Go to original source...
  24. Kowalski A., Palyga J. (2014): Polymorphic linker histone H1 variants in breeding and conservative duck populations. Annals of Animal Science, 14, 33-42. Go to original source...
  25. Kowalski A., Palyga J., Gornicka-Michalska E., Krajewska W.M. (1998): Allelic polymorphism of histone H1.a in duck erythrocytes. Biochemical Genetics, 36, 183-191. Go to original source... Go to PubMed...
  26. Kowalski A., Palyga J., Gornicka-Michalska E. (2008): Polymorphic isoforms of erythrocyte histone H1.a' in a Grey partridge population. Journal of Agrobiology, 25, 125-127.
  27. Kowalski A., Palyga J., Gornicka-Michalska E., Bernacki Z., Adamski M. (2010): Phenotypic variation of erythrocyte linker histone H1.c in a pheasant (Phasianus colchicus L.) population. Genetics and Molecular Biology, 33, 475-478. Go to original source... Go to PubMed...
  28. Kowalski A., Palyga J., Gornicka-Michalska E. (2011a): Two polymorphic linker histone loci in Guinea fowl erythrocyte. Comptes Rendus Biologies, 334, 6-12. Go to original source... Go to PubMed...
  29. Kowalski A., Palyga J., Gornicka-Michalska E. (2011b): Linker histone H1.b is polymorphic in grey partridge (Perdix perdix). Zeitschrift für Naturforschung C, 66, 296-304. Go to original source... Go to PubMed...
  30. Kratzmeier M., Albig W., Meergans T., Doenecke D. (1999): Changes in the protein pattern of H1 histones associated with apoptotic DNA fragmentation. Biochemical Journal, 337, 319-327. Go to original source...
  31. Lee H., Habas L., Abate-Shen C. (2004): Msx1 cooperates with histone H1b for inhibition of transcription and myogenesis. Science, 304, 1675-1678. Go to original source... Go to PubMed...
  32. Lu X., Hamkalo B., Parseghian M.H., Hansen J.C. (2009): Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry, 48, 164-172. Go to original source... Go to PubMed...
  33. Lu X., Wontakal S.N., Kavi H., Kim B.J., Guzzardo P.M., Emelyanov A.V., Xu N., Hannon G.J., Zavadil J., Fyodorov D.V., Skoultchi A.I. (2013): Drosophila H1 regulates the genetic activity of heterochromatin by recruitment of Su(var)3-9. Science, 340, 78-81. Go to original source... Go to PubMed...
  34. McBryant S.J., Lu X., Hansen J.C. (2010): Multifunctionality of the linker histones: an emerging role for protein-protein interactions. Cellular Research, 20, 519-528. Go to original source... Go to PubMed...
  35. Montes de Oca R., Lee K.K., Wilson K.L.L. (2005): Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones H1.1. Journal of Biological Chemistry, 280, 42252-42262. Go to original source... Go to PubMed...
  36. Neelin J.M., Neelin E.M., Lindsay D.W., Palyga J., Nichols C.R., Cheng K.M. (1995): The occurrence of a mutant dimerizable histone H5 in Japanese quail erythrocytes. Genome, 38, 982-990. Go to original source... Go to PubMed...
  37. Palyga J. (1991): A comparison of the histone H1 complements of avian erythrocytes. International Journal of Biochemistry, 23, 845-849. Go to original source... Go to PubMed...
  38. Palyga J. (1998a): Genes for polymorphic H1 histones are linked in the Japanese Quail genome. Biochemical Genetics, 36, 93-103. Go to original source... Go to PubMed...
  39. Palyga J. (1998b): Distribution of allelic forms of erythrocyte H1 histones in Japanase quail populations divergently selected for amount of weight loss after transient starvation. Biochemical Genetics, 36, 79-92. Go to original source... Go to PubMed...
  40. Palyga J., Gornicka-Michalska E., Kowalski A. (1993): Genetic polymorphism of histone H1.z in duck erythrocytes. Biochemical Journal, 294, 859-863. Go to original source... Go to PubMed...
  41. Palyga J., Gornicka-Michalska E., Kowalski A., Ksiazkiewicz J. (2000): Natural allelic variation of duck erythrocyte histone H1.b. International Journal of Biochemistry and Cell Biology, 32, 665-675. Go to original source... Go to PubMed...
  42. Parseghian M.H., Hamkalo B.A. (2001): A compendium of histone H1 family of somatic subtypes: an elusive cast of characters and their characteristics. Biochemistry and Cell Biology, 79, 289-304. Go to original source...
  43. Peng Z., Mizianty M.J., Xue B., Kurgan L., Uversky V.N. (2012): More than just tails: intrinsic disorder in histone proteins. Molecular Biosystems, 8, 1886-1898. Go to original source... Go to PubMed...
  44. Raghuram N., Carrero G., Th'ng J., Hendzel M.J. (2009): Molecular dynamics of histone H1. Biochemistry and Cell Biology, 87, 189-206. Go to original source... Go to PubMed...
  45. Sancho M., Diani E., Beato M., Jordan A. (2008): Depletion of human histone H1 variants uncovers specific roles in gene expression and cell growth. PLoS Genetics, 4, 1-17. Go to original source... Go to PubMed...
  46. Sarg B., Green A., Soderkvist B., Helliger W., Runquist I., Lindner H. (2005): Characterization of sequence variations in human histone H1.2 and H1.4 subtypes. FEBS Journal, 272, 3673-3683. Go to original source... Go to PubMed...
  47. Shannon M.F., Wells J.R.E. (1987): Characterization of the six chicken histone H1 proteins and alignment with their respective genes. Journal of Biological Chemistry, 262, 9664-9668. Go to original source...
  48. Takata H., Matsuanga S., Morimoto A., Ono-Maniwa R., Uchiyama S., Fukui K. (2007): H1.X with different properties from other linker histones is required for mitotic progression. FEBS Letters, 581, 3783-3788. Go to original source... Go to PubMed...
  49. Trollope A., Sapojnikova N., Thorne A.W., Crane-Robinson C., Myers F.A. (2010): Linker histone subtypes are not generalized gene repressors. Biochimica et Biophysica Acta, 1799, 642-652. Go to original source... Go to PubMed...
  50. Villar-Garea A., Imhof A. (2008): Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster. PLoS One, 3: e1553. Go to original source... Go to PubMed...

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