메뉴 건너뛰기




Volumn 273, Issue 6, 2006, Pages 1240-1250

Sequence variants of chicken linker histone H1.a

Author keywords

Allelic isoforms; Chicken; Genetic polymorphism; Histone H1; Peptide microsequencing

Indexed keywords

HISTONE H1;

EID: 33644755866     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05147.x     Document Type: Article
Times cited : (14)

References (51)
  • 1
    • 0023429583 scopus 로고
    • Microheterogeneity in H1 histones and its consequences
    • Cole RD 1987 Microheterogeneity in H1 histones and its consequences Int J Pept Protein Res 30 433 449
    • (1987) Int J Pept Protein Res , vol.30 , pp. 433-449
    • Cole, R.D.1
  • 3
    • 0035854055 scopus 로고    scopus 로고
    • Histone H1 diversity: Bridging regulatory signals to linker histone function
    • Khochbin S 2001 Histone H1 diversity: bridging regulatory signals to linker histone function Gene 271 1 12
    • (2001) Gene , vol.271 , pp. 1-12
    • Khochbin, S.1
  • 5
    • 0034881774 scopus 로고    scopus 로고
    • A compendium of the histone H1 family of somatic subtypes: An elusive cast of characters and their characteristics
    • Parseghian MH Hamkalo BA 2001 A compendium of the histone H1 family of somatic subtypes: an elusive cast of characters and their characteristics Biochem Cell Biol 79 289 304
    • (2001) Biochem Cell Biol , vol.79 , pp. 289-304
    • Parseghian, M.H.1    Hamkalo, B.A.2
  • 6
    • 0031574027 scopus 로고    scopus 로고
    • Differential effect of H1 variant overproduction on gene expression is due to differences in the central globular domain
    • Brown DT Gunjan A Alexander BT Sittman DB 1997 Differential effect of H1 variant overproduction on gene expression is due to differences in the central globular domain Nucleic Acids Res 25 5003 5009
    • (1997) Nucleic Acids Res , vol.25 , pp. 5003-5009
    • Brown, D.T.1    Gunjan, A.2    Alexander, B.T.3    Sittman, D.B.4
  • 7
    • 0037490067 scopus 로고    scopus 로고
    • Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone
    • Downs JA Kosmidou E Morgan A Jackson SP 2003 Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone Mol Cell 11 1685 1692
    • (2003) Mol Cell , vol.11 , pp. 1685-1692
    • Downs, J.A.1    Kosmidou, E.2    Morgan, A.3    Jackson, S.P.4
  • 9
    • 19644400009 scopus 로고    scopus 로고
    • The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA Fragmentation Factor (DFF40/CAD) and stimulates DNA cleavage
    • Widlak P Kalinowska M Parseghian MH Lu X Hansen JC Garrard WT 2005 The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA Fragmentation Factor (DFF40/CAD) and stimulates DNA cleavage Biochemistry 44 7871 7878
    • (2005) Biochemistry , vol.44 , pp. 7871-7878
    • Widlak, P.1    Kalinowska, M.2    Parseghian, M.H.3    Lu, X.4    Hansen, J.C.5    Garrard, W.T.6
  • 10
    • 15544369819 scopus 로고    scopus 로고
    • Suppression of histone H1 genes in Arabidopsis results in heritable developmental defects and stochastic changes in DNA methylation
    • Wierzbicki AT Jerzmanowski A 2005 Suppression of histone H1 genes in Arabidopsis results in heritable developmental defects and stochastic changes in DNA methylation Genetics 169 997 1008
    • (2005) Genetics , vol.169 , pp. 997-1008
    • Wierzbicki, A.T.1    Jerzmanowski, A.2
  • 13
    • 2942696668 scopus 로고    scopus 로고
    • MSX1 cooperates with histone H1b for inhibition of transcription and myogenesis
    • Lee H Habas R Abate-Shen C 2004 MSX1 cooperates with histone H1b for inhibition of transcription and myogenesis Science 304 1675 1678
    • (2004) Science , vol.304 , pp. 1675-1678
    • Lee, H.1    Habas, R.2    Abate-Shen, C.3
  • 14
    • 0035033040 scopus 로고    scopus 로고
    • A single histone H1 isoform (H1.1) is essential for chromatin silencing and germline development in Caenorhabditis elegans
    • Jedrusik MA Schulze E 2001 A single histone H1 isoform (H1.1) is essential for chromatin silencing and germline development in Caenorhabditis elegans Development 128 1069 1080
    • (2001) Development , vol.128 , pp. 1069-1080
    • Jedrusik, M.A.1    Schulze, E.2
  • 15
    • 0037965571 scopus 로고    scopus 로고
    • Telomeric position effect variegation in Saccharomyces cerevisiae by Caenorhabditis elegans linker histones suggests a mechanistic connection between germ line and telomeric silencing
    • Jedrusik MA Schulze E 2003 Telomeric position effect variegation in Saccharomyces cerevisiae by Caenorhabditis elegans linker histones suggests a mechanistic connection between germ line and telomeric silencing Mol Cell Biol 23 3681 3691
    • (2003) Mol Cell Biol , vol.23 , pp. 3681-3691
    • Jedrusik, M.A.1    Schulze, E.2
  • 16
    • 0035903114 scopus 로고    scopus 로고
    • Induction of secondary structure in a COOH-terminal peptide of histone H1 by interaction with the DNA: An infrared spectroscopy study
    • Vila R Ponte I Collado M Arrondo JL Suau P 2001 Induction of secondary structure in a COOH-terminal peptide of histone H1 by interaction with the DNA: an infrared spectroscopy study J Biol Chem 276 30898 30903
    • (2001) J Biol Chem , vol.276 , pp. 30898-30903
    • Vila, R.1    Ponte, I.2    Collado, M.3    Arrondo, J.L.4    Suau, P.5
  • 17
  • 18
    • 0037357480 scopus 로고    scopus 로고
    • Sequence complexity of histone H1 subtypes
    • Ponte I Vila R Suau P 2003 Sequence complexity of histone H1 subtypes Mol Biol Evol 20 371 380
    • (2003) Mol Biol Evol , vol.20 , pp. 371-380
    • Ponte, I.1    Vila, R.2    Suau, P.3
  • 19
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • Hendzel MJ Lever MA Crawford E Th'ng JP 2004 The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo J Biol Chem 279 20028 20034
    • (2004) J Biol Chem , vol.279 , pp. 20028-20034
    • Hendzel, M.J.1    Lever, M.A.2    Crawford, E.3    Th'ng, J.P.4
  • 20
    • 23044489675 scopus 로고    scopus 로고
    • H1 family histones in the nucleus: Control of binding and localization by the C-terminal domain
    • Th'ng JP Sung R Ye M Hendzel MJ 2005 H1 family histones in the nucleus: control of binding and localization by the C-terminal domain J Biol Chem 280 27809 27814
    • (2005) J Biol Chem , vol.280 , pp. 27809-27814
    • Th'Ng, J.P.1    Sung, R.2    Ye, M.3    Hendzel, M.J.4
  • 21
    • 0020161243 scopus 로고
    • Molecular variants of histone H5 of linnet (Acanthis flammea)
    • (in Russian).
    • Gorel FL Berdnikov VA Rozov SM 1982 Molecular variants of histone H5 of linnet (Acanthis flammea) Mol Biol (Mosk) 16 790 798 (in Russian).
    • (1982) Mol Biol (Mosk) , vol.16 , pp. 790-798
    • Gorel, F.L.1    Berdnikov, V.A.2    Rozov, S.M.3
  • 24
    • 0242493872 scopus 로고    scopus 로고
    • Large changes in the structure of the major histone H1 subtype result in small effects on quantitative traits in legumes
    • Berdnikov VA Bogdanova VS Gorel FL Kosterin OE Trusov YA 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
    • (2003) Genetica , vol.119 , pp. 167-182
    • Berdnikov, V.A.1    Bogdanova, V.S.2    Gorel, F.L.3    Kosterin, O.E.4    Trusov, Y.A.5
  • 25
    • 20444487430 scopus 로고    scopus 로고
    • Structure of allelic variants of subtype 5 of histone H1 in pea Pisum sativum L
    • Bogdanova VS Lester DR Berdnikov VA Andersson I 2005 Structure of allelic variants of subtype 5 of histone H1 in pea Pisum sativum L Heredity 94 582 588
    • (2005) Heredity , vol.94 , pp. 582-588
    • Bogdanova, V.S.1    Lester, D.R.2    Berdnikov, V.A.3    Andersson, I.4
  • 26
  • 27
    • 0015238014 scopus 로고
    • Heterogeneity and polymorphism in chicken erythrocyte histone fraction V
    • Greenaway PJ Murray K 1971 Heterogeneity and polymorphism in chicken erythrocyte histone fraction V Nat New Biol 229 233 238
    • (1971) Nat New Biol , vol.229 , pp. 233-238
    • Greenaway, P.J.1    Murray, K.2
  • 29
    • 0028146985 scopus 로고
    • Phenotypic effect of substitutions of short chromosomal segments containing different alleles of histone H1 genes in garden pea (Pisum sativum L.)
    • Bogdanova VS Rozov SM Trusov YA Berdnikov VA 1994 Phenotypic effect of substitutions of short chromosomal segments containing different alleles of histone H1 genes in garden pea (Pisum sativum L.) Genet Res 64 35 41
    • (1994) Genet Res , vol.64 , pp. 35-41
    • Bogdanova, V.S.1    Rozov, S.M.2    Trusov, Y.A.3    Berdnikov, V.A.4
  • 30
    • 0031826547 scopus 로고    scopus 로고
    • Distribution of allelic forms of erythrocyte H1 histones in Japanese quail populations divergently selected for amount of weight loss after transient starvation
    • Pałyga J 1998 Distribution of allelic forms of erythrocyte H1 histones in Japanese quail populations divergently selected for amount of weight loss after transient starvation Biochem Genet 36 79 92
    • (1998) Biochem Genet , vol.36 , pp. 79-92
    • Pałyga, J.1
  • 32
    • 0027431393 scopus 로고
    • Genetic polymorphism of histone H1.z in duck erythrocytes
    • Pałyga J Górnicka-Michalska E Kowalski A 1993 Genetic polymorphism of histone H1.z in duck erythrocytes Biochem J 294 859 863
    • (1993) Biochem J , vol.294 , pp. 859-863
    • Pałyga, J.1    Górnicka-Michalska, E.2    Kowalski, A.3
  • 34
    • 0031875045 scopus 로고    scopus 로고
    • Genes for polymorphic H1 histones are linked in the Japanese quail genome
    • Pałyga J 1998 Genes for polymorphic H1 histones are linked in the Japanese quail genome Biochem Genet 36 93 103
    • (1998) Biochem Genet , vol.36 , pp. 93-103
    • Pałyga, J.1
  • 35
    • 7344236021 scopus 로고    scopus 로고
    • Isolation and preliminary characterization of histone H1.b allelic variants from quail erythrocytes
    • Pałyga J Neelin JM 1998 Isolation and preliminary characterization of histone H1.b allelic variants from quail erythrocytes Genome 41 709 719
    • (1998) Genome , vol.41 , pp. 709-719
    • Pałyga, J.1    Neelin, J.M.2
  • 37
    • 0023655380 scopus 로고
    • Characterization of the six chicken histone H1 proteins and alignment with their respective genes
    • Shannon MF Wells JR 1987 Characterization of the six chicken histone H1 proteins and alignment with their respective genes J Biol Chem 262 9664 9668
    • (1987) J Biol Chem , vol.262 , pp. 9664-9668
    • Shannon, M.F.1    Wells, J.R.2
  • 38
    • 0023655645 scopus 로고
    • Characterization of the chicken histone H1 gene complement: Generation of a complete set of vertebrate H1 protein sequences
    • Coles LS Robins AJ Madley LK Wells JR 1987 Characterization of the chicken histone H1 gene complement: generation of a complete set of vertebrate H1 protein sequences J Biol Chem 262 9656 9663
    • (1987) J Biol Chem , vol.262 , pp. 9656-9663
    • Coles, L.S.1    Robins, A.J.2    Madley, L.K.3    Wells, J.R.4
  • 39
    • 14644388222 scopus 로고    scopus 로고
    • The dynamics of histone H1 function in chromatin
    • Bustin M Catez F Lim JH 2005 The dynamics of histone H1 function in chromatin Mol Cell 17 617 620
    • (2005) Mol Cell , vol.17 , pp. 617-620
    • Bustin, M.1    Catez, F.2    Lim, J.H.3
  • 40
    • 1942502862 scopus 로고    scopus 로고
    • Different Ezh2-containing complexes target methylation of histone H1 or nucleosomal histone H3
    • Kuzmichev A Jenuwein T Tempst P Reinberg D 2004 Different Ezh2-containing complexes target methylation of histone H1 or nucleosomal histone H3 Mol Cell 14 183 193
    • (2004) Mol Cell , vol.14 , pp. 183-193
    • Kuzmichev, A.1    Jenuwein, T.2    Tempst, P.3    Reinberg, D.4
  • 41
    • 33646569673 scopus 로고    scopus 로고
    • Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: Identification of a novel phosphorylation site on histone H1
    • doi: 10.1074/jbc.M508957200.q5
    • Sarg B Helliger W Talasz H Forg B Lindner HH 2005 Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1 J Biol Chem doi: 10.1074/jbc.M508957200.q5
    • (2005) J Biol Chem
    • Sarg, B.1    Helliger, W.2    Talasz, H.3    Forg, B.4    Lindner, H.H.5
  • 42
    • 84966155914 scopus 로고
    • Geographic patterns of histone H1 allelic frequencies formed in the course of Pisum sativum L. (pea) cultivation
    • Berdnikov VA Bogdanova VS Rozov SM Kosterin OE 1993 Geographic patterns of histone H1 allelic frequencies formed in the course of Pisum sativum L. (pea) cultivation Heredity 71 199 209
    • (1993) Heredity , vol.71 , pp. 199-209
    • Berdnikov, V.A.1    Bogdanova, V.S.2    Rozov, S.M.3    Kosterin, O.E.4
  • 44
    • 29144529317 scopus 로고    scopus 로고
    • Binding of barrier-to-autointegration factor (BAF) to histone H3 and selected linker histones including H1.1
    • Montes de Oca R Lee KK Wilson KL 2005 Binding of barrier-to- autointegration factor (BAF) to histone H3 and selected linker histones including H1.1 J Biol Chem 280 42252 42262
    • (2005) J Biol Chem , vol.280 , pp. 42252-42262
    • Montes De Oca, R.1    Lee, K.K.2    Wilson, K.L.3
  • 45
    • 0024465335 scopus 로고
    • SPKK, a new nucleic acid-binding unit of protein found in histone
    • Suzuki M 1989 SPKK, a new nucleic acid-binding unit of protein found in histone EMBO J 8 797 804
    • (1989) EMBO J , vol.8 , pp. 797-804
    • Suzuki, M.1
  • 46
    • 0033637116 scopus 로고    scopus 로고
    • Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch
    • Dou Y Gorovsky MA 2000 Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch Mol Cell 6 225 231
    • (2000) Mol Cell , vol.6 , pp. 225-231
    • Dou, Y.1    Gorovsky, M.A.2
  • 47
    • 0037144862 scopus 로고    scopus 로고
    • Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin
    • Dou Y Bowen J Liu Y Gorovsky MA 2002 Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin J Cell Biol 158 1161 1170
    • (2002) J Cell Biol , vol.158 , pp. 1161-1170
    • Dou, Y.1    Bowen, J.2    Liu, Y.3    Gorovsky, M.A.4
  • 48
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T Allis CD 2001 Translating the histone code Science 293 1074 1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 49
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: Causes, effects and implications of Hsp90-mediated genetic capacitance
    • Sangster TA Lindquist S Queitsch C 2004 Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance Bioessays 26 348 362
    • (2004) Bioessays , vol.26 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 50
    • 13244295625 scopus 로고    scopus 로고
    • Association of NASP with HSP90 in mouse spermatogenic cells: Stimulation of ATPase activity and transport of linker histones into nuclei
    • Alekseev OM Widgren EE Richardson RT O'Rand MG 2005 Association of NASP with HSP90 in mouse spermatogenic cells: stimulation of ATPase activity and transport of linker histones into nuclei J Biol Chem 280 2904 2911
    • (2005) J Biol Chem , vol.280 , pp. 2904-2911
    • Alekseev, O.M.1    Widgren, E.E.2    Richardson, R.T.3    O'Rand, M.G.4
  • 51
    • 0017622805 scopus 로고
    • Methods for isolation of nuclei and nucleoli
    • Busch H Daskal Y 1977 Methods for isolation of nuclei and nucleoli Methods Cell Biol 15 1 43
    • (1977) Methods Cell Biol , vol.15 , pp. 1-43
    • Busch, H.1    Daskal, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.