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Allelic isoforms of the chicken and duck histone H1.a

Cellular & Molecular Biology Letters volume 19, pages 116–125 (2014)Cite this article

Abstract

Two isoforms of the erythrocyte histone H1.a were identified in two conservative flocks of Rhode Island Red chickens and six conservative flocks of ducks. The H1.a1 and H1.a2 isoforms formed three phenotypes (a1, a2 and a1a2) and were electrophoretically similar in the two species. The frequency of phenotype and histone H1.a allele occurrence varied within the genetic groups of birds, but the relatively rare allele a 2 was only detected in chicken and duck strains with colored feathers. Using mass spectrometry, we established that the difference between the measured masses of the duck H1.a isoforms was 156 Da. Since this value corresponds to the mass of the arginine residue alone or to the combined mass of the valine and glycine residues, we believe that the polymorphism of duck histone H1.a might have originated from sequence variation. A mass difference of 1 Da observed between chicken H1.a isoforms corresponded well to the previously detected Glu/Lys substitution (0.9414 Da) at position 117.

Abbreviations

PMSF:

phenylmethylsulfonyl fluoride

PVDF:

polyvinylidene fluoride

SDS:

sodium dodecyl sulfate

References

  1. Happel, N. and Doenecke, D. Histone H1 and its isoforms: contribution to chromatin structure and function. Gene 431 (2009) 1–12.

    Article  PubMed  CAS  Google Scholar 

  2. Fan, Y., Nikitina, T., Zhao, J., Fleury, T.J., Bhattacharyya, R., Bouhassira, E.E, Stein, A., Woodcock, C.L. and Skoultchi, A.I. Histone H1 depletion in mammals alter global chromatin structure but causes specific changes in gene regulation. Cell 123 (2005) 1199–1212.

    Article  PubMed  CAS  Google Scholar 

  3. Terme, J-M., Sese, B., Millan-Arino, L., Mayor, R., Izpisua Belmonte, J.C., Barrero, M.J. and Jordan, A. Histone H1 variants are differently expressed and incorporated into chromatin during differentiation and reprogramming to pluripotency. J. Biol. Chem. 286 (2011) 35347–35357.

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  4. Parseghian, M.H. and Hamkalo, B.A. A compendium of the histone H1 family of somatic subtypes: An elusive cast of characters and their characteristics. Biochem. Cell. Biol. 79 (2001) 289–304.

    Article  PubMed  CAS  Google Scholar 

  5. Izzo, A., Kamieniarz, K. and Schneider, R. The histone H1 family: specific members, specific functions? Biol. Chem. 389 (2008) 333–343.

    Article  PubMed  CAS  Google Scholar 

  6. McBryant, S.J., Lu, X. and Hansen, J.C. Multifunctionality of the linker histones: an emerging role for protein-protein interactions. Cell. Res. 20 (2010) 519–528.

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  7. Jerzmanowski, A. The linker histones, In: Zlatanova, J., Leuba, S., (Eds.), Chromatin structure & dynamics: State-of-the-Art. Elsevier Science BV, 2004, 75–102.

    Chapter  Google Scholar 

  8. Kowalski, A., Pałyga, J., Górnicka-Michalska, E. and Krajewska, W.M. Allelic polymorphism of histone H1.a in duck erythrocytes. Biochem. Genet. 36 (1998) 183–191.

    Article  PubMed  CAS  Google Scholar 

  9. Górnicka-Michalska, E, Pałyga, J, Kowalski, A. and Cywa-Benko K. Sequence variants of chicken linker histone H1.a. FEBS J. 273 (2006) 1240–1250.

    Article  PubMed  CAS  Google Scholar 

  10. Coles, L.S., Robins, A.J., Madley, L.K. and Wells, R.S. Characterization of the chicken histone H1 gene complement. Generation of a complete set of vertebrate H1 protein sequences. J. Biol. Chem. 262 (1987) 9656–9663.

    PubMed  CAS  Google Scholar 

  11. Pałyga, J., Górnicka-Michalska, E. and Kowalski, A. Genetic polymorphism of histone H1.z in duck erythrocytes. Biochem J. 294 (1993) 859–863.

    PubMed Central  PubMed  Google Scholar 

  12. Kowalski, A. and Pałyga, J. 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, In Tech, 2012, 117–136.

    Google Scholar 

  13. Mizzen, C.A., Alpert, A.J., Levesque, L., Kruck, T.P.A. and McLachlan, D.R. Resolution of allelic and non-allelic variants of histone H1 by cationexchange-hydrophilic-interaction chromatography. J. Chromatogr. B 744 (2000) 33–46.

    Article  CAS  Google Scholar 

  14. Sarg, B., Green, A., Soderkvist, B., Helliger, W., Runquist, I. and Lindner, H. Characterization of sequence variations in human histone H1.2 and H1.4 subtypes. FEBS J. 272 (2005) 3673–3683.

    Article  PubMed  CAS  Google Scholar 

  15. Ortiz, M.L., Calero, M., Fernandez Patron, C., Patron, C.F., Castellanos, L. and Mendez, L. Imidazole-SDS-Zn reverse staining of proteins in gels containing or not SDS and microsequence of individual unmodified electroblotted proteins. FEBS Lett. 296 (1992) 300–304.

    Article  PubMed  CAS  Google Scholar 

  16. Cohen, S.L. and Chait, B.T. Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. Anal. Biochem. 247 (1997) 257–267.

    Article  PubMed  CAS  Google Scholar 

  17. Villar-Garea, A. and Imhof, A. Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster. PLoS One (2008) e1553. doi:10.1371/journal.pone.00015531-11.

    Google Scholar 

  18. Berdnikov, V.A., Bogdanova, V.S., Gorel, F.L., Kosterin, O.E. and Trusov, Y.A. Large changes in the structure of the major histone H1 subtype result in small effects on quantitative traits in legumes. Genetica 119 (2003) 67–182.

    Article  Google Scholar 

  19. Wisniewski, J.R., Zougman, A., Kruger, S. and Mann, M. Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol. Cell. Proteomics 6 (2007) 72–87.

    Article  PubMed  CAS  Google Scholar 

  20. Routh, A., Sandin, S. and Rhodes, D. Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure. Proc. Natl. Acad. Sci. USA 105 (2008) 8872–8877.

    Article  PubMed Central  PubMed  Google Scholar 

  21. Zlatanova, J., Caiafa, P. and van Holde, K. Linker histone binding and displacement: versatile mechanism for transcriptional regulation. FASEB J. 14 (2000) 1697–1704.

    Article  PubMed  CAS  Google Scholar 

  22. Trollope, A., Sapojnikova, N., Thorne, A.W., Crane-Robinson, C. and Myers, F.A. Linker histone subtypes are not generalized gene repressors. Biochem. Biophys. Acta 1799 (2010) 642–652.

    PubMed  CAS  Google Scholar 

  23. Caterino, T.L., Fang, H. and Hayes, J.J. Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain. Mol. Cell. Biol. 31 (2011) 2341–2348.

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  24. Hansen, J.C., Lu, X., Ross, E.D. and Woody, R.W. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J. Biol. Chem. 281 (2006) 1853–18656.

    Article  PubMed  CAS  Google Scholar 

  25. Lu, X., Hamkalo, B., Parseghian, M.H. and Hansen, J.C. Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry 48 (2009) 164–172.

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  26. Bogdanova, V.S., Lester, D.R., Berdnikov, V.A. and Andersson, I. Structure of allelic variants of subtype 5 of histone H1 in a pea Pisum sativum L. Heredity 94 (2005) 582–588.

    Article  PubMed  CAS  Google Scholar 

  27. Bogdanova, V.S., Kosterin, O.E. and Berdnikov, V.A. 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 (2007) 61–72.

    Article  PubMed  Google Scholar 

  28. Pałyga, J., Górnicka-Michalska, E., Kowalski, A., Książkiewicz, J. Natural allelic variation of duck erythrocyte histone H1.b. Int. J. Biochem. Cell Biol. 32 (2000) 665–675.

    Article  PubMed  Google Scholar 

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Authors and Affiliations

  1. Department of Biochemistry and Genetics, Institute of Biology, Jan Kochanowski University, ul. Świętokrzyska 15, 25-406, Kielce, Poland

    Ewa Górnicka-Michalska, Andrzej Kowalski & Jan Pałyga

Authors
  1. Ewa Górnicka-Michalska
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  2. Andrzej Kowalski
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  3. Jan Pałyga
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Correspondence to Andrzej Kowalski.

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Górnicka-Michalska, E., Kowalski, A. & Pałyga, J. Allelic isoforms of the chicken and duck histone H1.a. Cell Mol Biol Lett 19, 116–125 (2014). https://doi.org/10.2478/s11658-014-0182-8

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Keywords

Cellular & Molecular Biology Letters

ISSN: 1689-1392

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