Linker histone subtypes and their allelic variants

Cell Biology International

Volumn 36, Issue 11, 2012, Pages 981-996

  Kowalski, Andrzej ^a   Pałyga, Jan ^a  

^a JAN KOCHANOWSKI UNIVERSITY   (Poland)

Author keywords

Histone H1 allelic isoforms; Histone H1 non allelic subtypes; Intrinsically disordered proteins; Polymorphism; Quantitative traits

Indexed keywords

HISTONE H1;

ALLELE; ARTICLE; CHROMATIN STRUCTURE; COMPLEX FORMATION; DNA STRUCTURE; GENE EXPRESSION REGULATION; GENE LOCATION; GENETIC ASSOCIATION; GENETIC POLYMORPHISM; GENETIC VARIABILITY; HUMAN; NONHUMAN; NUCLEAR REPROGRAMMING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; QUANTITATIVE TRAIT; SEQUENCE HOMOLOGY;

ALLELES; ANIMALS; CHROMATIN; CHROMATIN ASSEMBLY AND DISASSEMBLY; DNA; GENETIC VARIATION; HISTONES; HUMANS; NUCLEOSOMES; NUCLEOTIDE MOTIFS; PLANTS; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 84867734829     PISSN: 10656995     EISSN: 10958355     Source Type: Journal    
DOI: 10.1042/CBI20120133     Document Type: Article

References (156)

1. Alami R, Fan Y, Pack S, Sonbuchner TM, Besse A, Lin Q et al. Mammalian linker-histone subtypes differently affect gene expression in vivo. Proc Natl Acad Sci USA 2003;100:5920-5.
2. Allan J, Mitchell T, Harborne N, Bohm L, Crane-Robinson C. Roles of H1 domains in determining higher order chromatin structure and H1 location. J Mol Biol 1986;187:591-601.
3. Allan J, Cowling GJ, Harborne R, Cattini P, Craigie R, Gould H. Regulation of the higher-order structure of chromatin by histone H1 and H5. J Cell Biol 1981;90:279-88.
4. Allan J, Hartman PG, Crane-Robinson C, Aviles FX. The structure of histone H1 and its location in chromatin. Nature 1980;288:675-9.
5. Ascenzi R, Garitt JS. Subnuclear distribution of the entire complement of linker histone variants in Arabidopsis thaliana. Chromosoma 1999;108:345-55.
6. Barra JL, Rhounim L, Rossignol JL, Faugeron G. Histone H1 is dispensable for methylation-associate gene silencing in Ascobolus immersus and essential for long life span. Mol Cell Biol 2000;20:61-9.
7. Bednar J, Horowitz RA, Grigoryev SA, Carruthers IM, HansenJC, Koster AJ et al. Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Proc Natl Acad Sci USA 1998;95:14173-8.
8. Belyaev AI, Berdnikov VA. Polymorphism and localization of H1 histone genes in pea (Pisum sativum L.). Genetika 1981;17:498-504 (in Russian).
9. Belyaev AI, Berdnikov VA. Intraspecific polymorphism of H1 histone in the wild Fabaceae species. Genetika 1985;21:605-13 (in Russian).
10. Berdnikov VA, Bogdanova VS, Gorel FL, Kosterin OE, Trusov YA. Large changes in the structure of the major histone H1 subtype result in small effects on quantitative traits in legumes. Genetica 2003;119:67-182.
11. Berdnikov VA, Gorel FL, Bogdanova VS, Kosterin OE, Trusov YA, Rozov SM. Effect of a substitution of a short chromosome segment carrying a histone H1 locus on expression of the homeotic gene Tl in heterozygote in the garden pea. Genet Res (Camb) 1999;73:93-109.
12. Berdnikov VA, Bogdanova VS, Rozov SM, Kosterin OE. Geographic patterns of histone H1 allelic frequencies formed in the course of Pisum sativum L. (pea) cultivation. Heredity 1993;71:199-209.
13. Berdnikov VA, Bogdanova VS, Gorel FL, Rozov SM. Territorial distribution of histone H1 alleles in a population of Vicia unijuga A.Br.formed after ubranization of natural habitat. Can J Bot 1992;70:1591-5.
14. Berdnikov VA, Bogdanova VS, Gorel FL, Rozov SM. Role of anthropogenic factor in a territorial distribution of histone H1 allelic variants in natural population of Vicia unijuga. Dokl Akad Nauk SSSR 1984;278:990-3 (in Russian).
15. Berdnikov VA, Gorel FL, Rodin SN. Intraspecific polymorphism of histone H5 in linnet Acanthis flammea. Dokl Akad Nauk SSSR 1983;271:732-6 (in Russian).
16. Berdnikov VA, Gorel FL, Argutinskaya SV, Cherepanova VA, Kilyeva EV. On the connection of the subfraction composition of histone H1 with the cell type in birds. Mol Biol (Mosc) 1976;10:887-96 (in Russian).
17. Berdnikov VA, Gorel FL. A study of ratios between histone fractions. Mol Biol (USSR) 1975:9:699-705 (in Russian).
18. Bogdanova VS, Kosterin OE, Berdnikov VA. Phenotypic effect of substitution of allelic variants for a histone H1 subtype specific for growing tissues in the garden pea (Pisum sativum L.). Genetica 2007;130:61-72.
19. Bogdanova VS, Lester DR, Berdnikov VA, Andersson I. Structure of allelic variants of subtype 5 of histone H1 in a pea Pisum sativum L. Heredity 2005;94:582-8.
20. Bogdanova VS, Rozov SM, Trusov YA, Berdnikov VA. Phenotypic effect of substitution of short chromosomal segments containing different alleles of histone H1 genes in garden pea (Pisum sativum L.). Genet Res (Camb) 1994;64:35-41.
21. Böhm L, Mitchell TC. Sequence conservation in the N-terminal domain of histone H1. FEBS Lett 1985;194:1-4.
22. Boix J, Mezquita C. Histone H1c decreases markedly in postreplicative stages of chicken spermatogenesis. Int J Dev Biol 1991;35: 43-8.
23. Briand G, Kmiecik D, Sautiere P, Wouters D, Borie-Loy O, Biserte G et al. Chicken erythrocyte histone H5.IV. Sequence of the carboxytermined half of the molecule (96 residues) and complete sequence. FEBS Lett 1980;112:147-51.
24. Brown DT, Izard T, Misteli T. Mapping the interaction surface of linker histone H1o with the nucleosome of native chromatin in vivo. Nat Struct Mol Biol 2006:13:250-5.
25. Brown DT, Alexander DT, Sittman DB. Differential effect of H1 variant overexpression on cell cycle progression and gene expression. Nucleic Acids Res 1996;24 486-93.
26. Caterino TL, Hayes JJ. Structure of the H1 C-terminal domain and function in chromatin condensation. Biochem Cell Biol 2011;89:35-44.
27. Catez F, Ueda T, Bustin M. Determinants of histone H1 mobility and chromatin binding in living cells. Nat Struct Mol Biol 2006,13:305-10.
28. Chen J, Kinyamu HK, Archer TK. Changes in attitude, changes in latitude; nuclear receptors remodeling chromatin to regulate transcription. Mol Endocrinol 2006;20:1-13.
29. Chen ZJ. Molecular mechanisms of polyploidy and hybrid vigor. Trends Plant Sci 2010;15:57-71.
30. Churchill MEA, Travers AA. Protein motifs that recognize structural features of DNA. Trends Biochem Sci 1991;16:92-7.
31. Clark DJ, Hill CS, Martin SR, Thomas JO. α-Helix in the carboxy-terminal domain of histone H1 and H5. EMBO J 1998;7:69-75.
32. Clausell J, Happel N, Hale TK, Doenecke D, Beato M. Histone H1 subtypes differently modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF. PLoS One 2009;4;e0007243.
33. Colavito-Shepanski M, Gorovsky MA. The histone content of Tetrahymena ribosomal gene-containing chromatin. J Biol Chem 1983;258:5944-54.
34. Cole RD. A minireview of microheterogeneity in H1 histone and its possible significance. Anal Biochem 1984;13:624-30.
35. Coles LS, Robins AJ, Madley LK, Wells JRE. Characterization of the chicken histone H1 gene complement. J Biol Chem 1987;262:9656-63.
36. Conn LK, Hendzel MJ, Schang LM. Linker histones are mobilized during infections with herpes simplex virus type 1. J Virol 2008;82:8629-46.
37. Croston GE, Kerrigan LA, Lira LM, Marshak DR, Kadonaga JT. Sequence-specific antirepression of histone H1-mediated inhibition of basal RNA polymerase II transcription. Science 1991;8:643-9.
38. Davis CF, Dorak MT. An extensive analysis of the hereditary hemochromatosis gene HFE and neighboring histone genes: associations with childhood leukemia. Ann Hematol 2010;89:375-84.
39. D'Erme M, Zardo G, Reale A, Caiafa P. Co-operative interaction of oligonucleosomal DNA with the H1e histone variant and its poly(ATP-ribosyl)ated isoform. Biochem J 1996;316:475-80.
40. Dominguez V, Pina B, Suau P. Histone H1 subtype synthesis in neurons and neuroblasts. Development 1992;115:181-5.
41. Dorigo B, Schalch T, Kulangara A, Duda S, Schroeder RR, Richmond TJ. Nucleosome arrays reveal the two-start organization of the chromatin fiber. Science 2004;306:1571-3.
42. Doenecke D, Albig W, Bouterfa H, Drabent B. Organization and expression of H1 histone and H1 replacement histone genes. J Cell Biochem 1994;54:423-31.
43. Downs JA, Kosmidou E, Morgan A, Jackson SP. Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone. Mol Cell 2003;11:1685-92.
44. Dudnikov AJ. Geographic patterns of histone H1 encoding genes allelic variation in Aegilops tauschii Coss. (Poaceae). Mol Biol Rep 2011;39:2355-63.
45. Fan Y, Nikitina T, Zhao J, Fleury TJ, Bhattacharyya R, Bouhassira EE et al. Histone H1 depletion in mammals alter global chromatin structure but causes specific changes in gene regulation. Cell 2005;123:1199-212.
46. Fan L, Roberts VA. Complex of linker histone H5 with the nucleosome and its implications for chromatin packing. Proc Natl Acad Sci USA 2006;103:8384-9.
47. Gabrilovich DJ, Cheng P, Fan Y, Yu B, Nikitina E, Sirotkin A et al. H1(0) histone and differentiation of dendric cells.A molecular target for tumor-derived factors. J Leukoc Biol 2002;72:285-96.
48. George EM, Izard T, Anderson SD, Brown DT. Nucleosome interaction surface of linker histone H1c is distinct from that of H10. J Biol Chem 2010;285:20891-6.
49. Georgel PT, Hansen JC. Linker histone function in chromatin: dual mechanism of action. Biochem Cell Biol 2001;79:3131-6.
50. Godde JS, Ura K. Cracking the enigmatic linker histone code. J Biochem 2008:143:287-303.
51. Gorel FL, Berdnikov VA, Rozov SM. Molecular variants of histone H5 of linnet (Acanthis flammea). Mol Biol (Mosc) 1982;16:790-8 (in Russian).
52. Górnicka-Michalska E, Pałyga J, Kowalski A, Cywa-Benko K. Sequence variants of chicken linker histone H1.a. FEBS J 2006;273:1240-50.
53. Górnicka-Michalska E, Pałyga J, LubońH, Kowalski A, Cywa-Benko K. Genetic variants of chicken erythrocyte histone H5. Biochem Mol Biol Int 1998;44:605-15.
54. Greenway PJ, Murray K. Heterogeneity and polymorphism in chicken erythrocyte histone fraction V. Nature New Biol 1971;229:233-8.
55. Gunjan A, Alexander BT, Sittman D, Brown DT. Effects of histone H1 variant overexpression on chromatin structure. J Biol Chem 1999;274:37950-6.
56. Hannon R, Bateman E, Allan J, Harborne R, Gould H. Control of RNA polymerase binding to chromatin by variations in linker histone composition. J Mol Biol 1984;180:131-49.
57. Hansen J, Lu X, Ross ED, Woody RW. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem 2006;281:1853-6.
58. Hansen J. Conformational dynamics of the chromatin fiber in solutions: determinants, mechanisms, and functions. Annu Rev Biophys Biomol Struct 2002;31:361-92.
59. Hayes JJ, Wolffe AP. Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome. Proc Natl Acad Sci USA 1993;90:6415-9.
60. Happel N, Doenecke D. Histone H1 and its isoforms: contribution to chromatin structure and function. Gene 2009;431:1-12.
61. Happel N, Warneboldt J, Hänecke K, Haller F, Doenecke D. H1 subtype expression during cell proliferation and growth arrest. Cell Cycle 2009;8:2226-32.
62. Hartman PG, Chapman GE, Moss T, Bradbury EM. Studies on the role and mode of operation of the very-lysine rich histone H1 in eukaryote chromatin. Eur J Biochem 1977;77:45-51.
63. Hendzel MJ, Lever MA, Crawford E, Th'ng JPH. The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. J Biol Chem 2004;279: 20028-34.
64. Higuraschi M, Adachi H, Ohba A. Synthesis and degradation of H1 histone subtypes in mouse lymphoma L5178Y cells. J Biol Chem 1987;262:13075-80.
65. Ishida T, Kinoshita K. PrDOS: prediction of disordered protein regions from amino acid sequence. Nucleic Acids Res 2007;35:460-4.
66. Izzo A, Kamieniarz K, Schneider R. The histone H1 family: specific members, specific functions? Biol Chem 2008;389:333-43.
67. Jedrusik M, Schulze E. A single histone H1 isoform (H1.1) is essential for chromatin silencing and germline development in Caenorhabditis elegans. Development 2001;128:1069-80.
68. Kasinsky HE, Lewis JD, Dacks JB, Ausio JO. Orgin of linker histones. FASEB J 2001;15: 34-42.
69. Khochbin S, Wolffe AP. Developmentally regulated expression of linkerhistone variants in vertebrates. Eur J Biochem 1994;225:50110.
70. Kosterin OE, Bogdanova VS, Gorel FL, Rozov SM, Trusov YA, Berdnikov VA. Histone H1 of the garden pea (Pisum sativum L.); composition, developmental changes, allelic polymorphism and inheritance. Plant Sci 1994;101:189-202.
71. Kowalski A, Pałyga J, Górnicka-Michalska E. Two polymorphic linker histone loci in Guinea fowl erythrocyte. CR Biol 2011a;334:6-12.
72. Kowalski A, Pałyga J, Górnicka-Michalska E. Linker histone H1.b is polymorphic in grey partridge (Perdix perdix). Z Naturforsch 2011b;66c;296-304.
73. Kowalski A, Pałyga J, Górnicka-Michalska E, Bernacki Z, Adamski M. Phenotypic variation of erythrocyte linker histone H1.c in a pheasant (Phasianus colchicus L.) population. Genet Mol Biol 2010;33:475-8.
74. Kowalski A, Pałyga J, Górnicka-Michalska E. Polymorphic isoforms of erythrocyte histone H1.a' in a Grey partridge population. J Agrobiol 2008;25:125-7.
75. Kowalski A, Pałyga J, Górnicka-Michalska E. Identification of histone H1.z components in a Muscovy duck (Cairina moschata L.) population. Comp Biochem Physiol B Biochem Mol Biol 2004;137:151-7.
76. Kowalski A, Pałyga J, Górnicka-Michalska E, Krajewska WM. Allelic polymorphism of histone H1.a in duck erythrocytes. Biochem Genet 1998;36:183-91.
77. Krieg PA, Robins AJ, Colman A, Wells JRE. Chicken histone H5 mRNA: the polyadenylated RNA lacks the conserved histone 39 terminator sequence. Nucleic Acids Res 1982;10:6777-85.
78. Latchman DS. Transcription factors: an overview. Int J Biochem Cell Biol 1997;29:1305-12.
79. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
80. Lennox RW, Cohen LH. The histone H1 complements of dividing and nondividing cells of the mouse. J Biol Chem 1983;258:262-8.
81. Lennox RW, Cohen LH. The production of tissue-specific histone complements during development. Biochem Cell Biol 1988;66:636-49.
82. Laybourn PJ, Kadonaga JT. Role of the nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II. Science 1991;254:238-45.
83. Li G, Reinberg D. Chromatin higher-order structures and gene regulation. Curr Opin Genet Dev 2011;21:175-86.
84. Lu X, Hamkalo B, Parseghian MH, Hansen JC. Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry 2009;48:164-72.
85. Lu X, Hansen JC. Identifications of specific functional subdomains within the linker histone H1 C-terminal domain. J Biol Chem 2004;279:8701-7.
86. Lu X, Hansen JC. Revisiting the structure and functions of the linker histone C-terminal tail domain. Biochem Cell Biol 2003;81:173-6.
87. Luger K, Mader AW, Richmond RR, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997;389:251-60.
88. Mackey-Cushman SL, Gao J, Holmes DA, Nunoya JI, Wang R, Unutmaz D, Su L. FoxP3 interacts with linker histone H1.5 to modulate gene expression and program Treg cell activity. Genes Immun 2011;12:559-67.
89. Marzluff WF, Gongidi P, Woods RK, Jin J, Maltais LJ. The human and mouse replication-dependent histone genes. Genomics 2002;80:487-98.
90. McBryant SJ, Lu X, Hansen JC. Multifunctionality of the linker histones: an emerging role for protein-protein interactions. Cell Res 2010;20:519-28.
91. Medvedev ZhA, Medvedeva MN, Robson L. Tissue specificity and age changes of the pattern of the H1 group of histones in chromatin from mouse tissues. Gerontology 1978;24:286-92.
92. Mizzen CA, Alpert AJ, Levesque L, Kruck TPA, McLachlan DR. Resolution of allelic and non-allelic variants of histone H1 by cationexchange-hydrophilic-interaction chromatography. J Chromatogr B 2000;774:33-46.
93. Mohr E, Trieschmann L, Grossbach U. Histone H1 in two subspecies of Chironomus thummi with different genome sizes: homologous chromosome sites differ largely in their content of a specific H1 variant. Proc Natl Acad Sci USA 1989;86:9308-12.
94. Nagel S, Grossbach U. Histone H1 genes and histone gene clusters in the genus Drosophila. J Mol Evol 2000;51:286-98.
95. Nishiyama M, Skoultchi AI, Nakayama KI. Histone H1 recruitment by CHD8 is essential for suppression of the Wnt-beta-catenin signaling pathway. Mol Cell Biol 2011;32:501-12.
96. Ohe Y, Hayashi H, Iwai K. Human spleen histone H1.Isolation and amino acid sequences of three minor variants H1a, H1c, and H1d. J Biochem 1989;106:844-57.
97. Pachov GV, Gabdoulline RR, Wade RC. On the structure and dynamics of the complex of the nucleosome and the linker histone. Nucleic Acids Res 2011;39:5255-63.
98. Pałyga J. Distribution of allelic forms of erythrocyte H1 histones in Japanase quail populations divergently selected for amount of weight loss after transient starvation. Biochem Genet 1998a;36:79-92.
99. Pałyga J. Genes for polymorphic H1 histones are linked in the Japanese quail genome. Biochem Genet 1998b;36:93-103.
100. Pałyga J. A comparison of the histone H1 complements of avian erythrocytes. Int J Biochem 1991a;23:845-9.
101. Pałyga J. Genetic polymorphism of histone H1.b in duck erythrocytes. Hereditas 1991b;114;85-9.
102. Pałyga J. Variability of histone H1 in rabbit populations. Int J Biochem 1990a;22:1351-61.
103. Pałyga J. Polymorphism of histone H1 in goose erythrocytes. Biochem Genet 1990b;28:359-65.
104. Pałyga J, Górnicka-Michalska E, Kowalski A, Ksia{ogonek}żkiewicz J. Natural allelic variation of duck erythrocyte histone H1.b. Int J Biochem Cell Biol 2000;32:665-75.
105. Pałyga J, Neelin JM. Isolation and preliminary characterization of histone H1.b allelic variants from quail erythrocytes. Genome 1998;41:709-19.
106. Pałyga J, Górnicka-Michalska E, Kowalski A. Genetic polymorphism of histone H1.z in duck erythrocytes. Biochem J 1993;294:859-63.
107. Panyim S, Chalkley R. High resolution acrylamide gel electrophoresis of histones. Arch Biochem Biophys 1969;130:337-46.
108. Parseghian ME, Newcomb RL, Winokur ST, Hamkalo BA. The distribution of somatic H1 subtypes is non-random on active vs.inactive chromatin: distribution of human fetal fibroblasts. Chromosome Res2000: 8;405-24.
109. Parseghian MH, Hamkalo BA. A compendium of histone H1 family of somatic subtypes: an elusive cast of characters and their characteristics. Biochem Cell Biol 2001;79:289-304.
110. Ponte I, Vidal-Taboada JM, Suau P. Evolution of the vertebrate H1 histone class: evidence for the functional differentiation of the subtypes. Mol Biol Evol 1998;15:702-8.
111. Raghuram N, Carrero G, Th'ng J, Hendzel MJ. Molecular dynamics of histone H1. Biochem Cell Biol 2009;87:189-206.
112. Ramakrishnan V, Finch JT, Graziano V, Lee PJ, Sweet RM. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 1993;362:219-23.
113. Risley MS, Eckhardt RA. H1 histone variants in Xenopus laevis. Dev Biol 1981;84:79-87.
114. Robinson PJJ, Rhodes D. Structure of the '30 nm' chromatin fibre: a key role for the linker histone. Curr Opin Struct Biol 2006;16;336-43.
115. Romero P, Obradovic Z, Li X, Garner EC, Brown CJ, Dunker AK. Sequence complexity of disordered protein. Protein Struct Funct Genet 2001;42:38-48.
116. Roque A, Ponte I, Suau P. Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1. J Phys Chem B 2009;113:12061-6.
117. Roque A, Iloro I, Ponte I, Arrondo JLR, Suau P. DNA-induced secondary structure of the carboxy-terminal domain of histone H1. J Biol Chem 2005;280:32141-7.
118. Sancho M, Diani E, Beato M, Jordan A. Depletion of human histone H1 variants uncovers specific roles in gene expression and cell growth. PLoS Genet 2008;4:e1000227.
119. Sarg B, Green A, Soderkvist B, Helliger W, Runquist I, Lindner H. Characterization of sequence variations in human histone H1.2 and H1.4 subtypes. FEBS J 2005;272:3673-83.
120. Schulze E, Trieschmann L, Schulze B, Schmidt ER, Pitzel S, Zechel K, Grossbach U. Structural and functional differences between histone H1 sequence variants with differential intracellular distribution. Proc Natl Acad Sci USA 1993;90:2481-5.
121. Shannon MF, Wells JRE. Characterization of the six chicken histone H1 proteins and alignment with their respective genes. J Biol Chem 1987;262:9664-8.
122. Simpson RT. Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry 1978;17:5524-31.
123. Steinbach OC, Wolffe AP, Rupp RA. Somatic linker histone cause loss of mesodermal competence in Xenopus. Nature 1997;389:395-9.
124. Stout JT, Phillips RL. Two independently inherited electrophoretic variants of the lysine-rich histone of maize (Zea mays). Proc Natl Acad Sci USA 1973;70:3043-7.
125. Subirana JA. Analysis of the charge distribution in the C-terminal region of histone H1 as rel.ted to its interaction with DNA. Biopolymers 1990;29:1351-7.
126. Suzuki M. SPKK, a new nucleic acid-binding unit of protein found in histone. EMBO J 1989;8:797-804.
127. Szerlong HJ, Hansen JC. Nucleosome distribution and linker DNA: connecting nuclear function to dynamics chromatin structure. Biochem Cell Biol 2011;89:24-34.
128. Takami Y, Nishi R, Nakayama T. Histone H1 variants play individual roles in transcription regulation in the DT40 chicken B cell line. Biochem Biophys Res Commun 2000;268:501-8.
129. Talasz H, Sapojnikova N, Helliger W, Lindner P, Puschendorf B. In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promoter. J Biol Chem. 1998;273:32236-43.
130. Talasz H, Helliger W, Puschendorf B, Lindner P. In vivo phosphorylation of histone H1 variants during the cell cycle. Biochemistry 1996;35:1761-7.
131. Tanaka H, Iguchi N, Isotani A, Kitamura K, Toyama Y, Matsuoka Y et al. HANP1/H1T2, a novel histone H1-like protein involved in nuclear formation and sperm fertility. Mol Cell Biol 2005;25:7107-19.
132. Terme J-M, Sese B, Millan-Arino L, Mayor R, Izpisua Belmonte JC, Barrero MJ et al. Histone H1 variants are differently expressed and incorporated into chromatin during differentiation and reprogramming to pluripotency. J Biol Chem 2011;286:35347-57.
133. Th'ng JPH, Sung R, Ye M, Hendzel MJ. H1 family histones in the nucleus.Control of binding and localization by the C-terminal domain. J Biol Chem 2005;280:27809-14.
134. Tompa P, Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 2008;33:2-8.
135. Tompa P, Szasz C, Buday L. Structural disorder throws new light on moonlighting. Trends Biochem Sci 2005;30:484-9.
136. Trollope A, Sapojnikova N, Thorne AW, Crane-Robinson C, Myers FA. Linker histone subtypes are not generalized gene repressors. Biochem Biophys Acta 2010;1799: 642-52.
137. Uversky VN. Intrinsically disordered proteins from A to Z. Int J Biochem Cell Biol 2011;43;1090-103.
138. van Holde K. Chromatin. New York, Springer Verlag; 1989.
139. Vicent GP, Nacht AS, Font-Mateu J, Castellano G, Gaveglia L, Ballare C et al. Four enzymes cooperate to displace histone H1 during the first minute of hormonal gene activation. Genes Dev 2011;25:845-62.
140. Vila R, Ponte I, Collado M, Arrondo JL, Suau P. Induction of secondary structure in a COOH-terminal peptide of histone H1 by interaction with the DNA: an infrared spectroscopy study. J Biol Chem 2001a;276:30898-903.
141. 2-terminal domain of histone H1. J Biol Chem 2001b;276:46429-35.
142. Vila R, Ponte I, Jimenez MA, Rico M, Suau P. A helix-turn motif in the C-terminal domain of histone H1. Protein Sci 2000;9:627-36.
143. Villar-Garea A, Imhof A. Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster. PLoS One 2008;3:e1553.
144. Vucetic S, Brown CJ, Dunker AK, Obradovic Z. Flavors of protein disorder. Protein Struct Funct Genet 2003;52:573-84.
145. Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdom of life. J Mol Biol 2004;377:635-43.
146. Widom J. Chromatin structure: linking structure to function with histone H1. Curr Biol 1998;8:788-91.
147. Wierzbicki AT, Jerzmanowski A. Suppression of histone H1 genes in Arabidopsis results in heritable developmental defects and stochastic changes in DNA methylation. Genetics 2005;169:997-1008.
148. Winter E, Levy D, Gordon JS. Changes in the histone H1 complement during myogenesis. I. Establishment by differential coupling of H-1 species synthesis to DNA replication. J Cell Biol 1985a;101:167-74.
149. Winter E, Palatnik CM, Williams DJ, Coles LS, Wells JRE, Gordon JS. Changes in the histone H1 complement during myogenesis.II. Regulation by differential coupling of H-1 variant mRNA accumulation to DNA replication. J Cell Biol 1985b;101:175-81.
150. Wong H, Victor J-M, Mozziconacci J. An all-atom model of the chromatin fiber containing linker histones reveals a versatile structure tuned by the nucleosomal repeat length. PLoS One 2007;2:e877.
151. Wood C, Snijders A, Williamson J, Reynolds C, Baldwin J, Dickman M. Post-translational modifications of the linker histone variants and their association with cell mechanisms. FEBS J 2009; 276:3685-97.
152. Wu J, Grunstein M. 25 years of the nucleosome model: chromatin modifications. Trends Biochem Sci 2000;25:619-23.
153. Yang S-H, Lee J, Lee S. Single nucleotide polymorphism in the promoter region of H1 histone family member N, testis-specific (H1FNT) and its association study with male infertility. Genomics Informatics 2010;8:201-5.
154. Yasuda H, Mueller RD, Logan KA, Bradbury EM. Identification of histone H1(0) in Physarum polycephalum.Its high level in the plasmodial stage increases in amount and phosphorylation in the sclerotial stage. J Biol Chem 1986;261:2349-54.
155. Zhou YB, Gerchman SE, Ramakrishnan V, Travers A, Muyldermans S. Position and orientation of the globular domain of linker histone H5 on the nucleosome. Nature 1998;395:402-5.
156. Zweidler A, Core histone variants of the mouse: primary structure and differential expression. In: Stein GS, Stein JL, Marzluff WF, editors. Histone genes: structure, organization and regulation, New York, John Wiley; 1984, pp. 339-71.