메뉴 건너뛰기




Volumn 9, Issue 6, 2014, Pages 791-797

dBigH1, a second histone H1 in Drosophila, and the consequences for histone fold nomenclature

Author keywords

Chromatin; Histone; Histone fold; Linker DNA; Nucleosome

Indexed keywords

HISTONE H1; CHROMATIN; DROSOPHILA PROTEIN; HISTONE; ISOPROTEIN;

EID: 84901802416     PISSN: 15592294     EISSN: 15592308     Source Type: Journal    
DOI: 10.4161/epi.28427     Document Type: Article
Times cited : (8)

References (69)
  • 1
    • 0035173870 scopus 로고    scopus 로고
    • Origin of H1 linker histones
    • PMID:11149891
    • Kasinsky HE, Lewis JD, Dacks JB, Ausió J. Origin of H1 linker histones. FASEB J 2001; 15:34-42; PMID:11149891; http://dx.doi.org/10.1096/ fj.00-0237rev
    • (2001) FASEB J , vol.15 , pp. 34-42
    • Kasinsky, H.E.1    Lewis, J.D.2    Dacks, J.B.3    Ausió, J.4
  • 2
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • PMID:8384699
    • Ramakrishnan V, Finch JT, Graziano V, Lee PL, Sweet RM. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 1993; 362:219-23; PMID:8384699; http://dx.doi.org/10.1038/362219a0
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 3
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • PMID:16301309
    • Hansen JC, Lu X, Ross ED, Woody RW. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem 2006; 281:1853-6; PMID:16301309; http://dx.doi.org/10.1074/jbc. R500022200
    • (2006) J Biol Chem , vol.281 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 4
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 A resolution: A tripartite protein assembly and a left-handed superhelix
    • PMID:1946434
    • Arents G, Burlingame RW, Wang BC, Love WE, Moudrianakis EN. The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix. Proc Natl Acad Sci U S A 1991; 88:10148-52; PMID:1946434; http://dx.doi.org/10.1073/pnas.88.22.10148
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 5
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • PMID:9305837
    • Luger K, Mäder AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997; 389:251-60; PMID:9305837; http://dx.doi. org/10.1038/38444
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 6
    • 84888330484 scopus 로고    scopus 로고
    • Structural insights into the histone H1-nucleosome complex
    • PMID:24218562
    • Zhou BR, Feng H, Kato H, Dai L, Yang Y, Zhou Y, Bai Y. Structural insights into the histone H1-nucleosome complex. Proc Natl Acad Sci U S A 2013; 110:19390-5; PMID:24218562; http://dx.doi. org/10.1073/pnas.1314905110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 19390-19395
    • Zhou, B.R.1    Feng, H.2    Kato, H.3    Dai, L.4    Yang, Y.5    Zhou, Y.6    Bai, Y.7
  • 7
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones
    • PMID:728412
    • Simpson RT. Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry 1978; 17:5524-31; PMID:728412; http://dx.doi.org/10.1021/ bi00618a030
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 8
    • 0021305320 scopus 로고
    • A minireview of microheterogeneity in H1 histone and its possible significance
    • PMID:6370036
    • Cole RD. A minireview of microheterogeneity in H1 histone and its possible significance. Anal Biochem 1984; 136:24-30; PMID:6370036; http://dx.doi. org/10.1016/0003-2697(84)90303-8
    • (1984) Anal Biochem , vol.136 , pp. 24-30
    • Cole, R.D.1
  • 9
    • 0033809749 scopus 로고    scopus 로고
    • Histone H1 genes and histone gene clusters in the genus Drosophila
    • PMID:11029073
    • Nagel S, Grossbach U. Histone H1 genes and histone gene clusters in the genus Drosophila. J Mol Evol 2000; 51:286-98; PMID:11029073
    • (2000) J Mol Evol , vol.51 , pp. 286-298
    • Nagel, S.1    Grossbach, U.2
  • 10
    • 33947524604 scopus 로고    scopus 로고
    • Histone variants--the structure behind the function
    • PMID:16772274
    • Ausió J. Histone variants--the structure behind the function. Brief Funct Genomic Proteomic 2006; 5:228-43; PMID:16772274; http://dx.doi. org/10.1093/bfgp/ell020
    • (2006) Brief Funct Genomic Proteomic , vol.5 , pp. 228-243
    • Ausió, J.1
  • 11
    • 84890085222 scopus 로고    scopus 로고
    • H1 histones: Current perspectives and challenges
    • PMID:23945933
    • Harshman SW, Young NL, Parthun MR, Freitas MA. H1 histones: current perspectives and challenges. Nucleic Acids Res 2013; 41:9593-609; PMID:23945933; http://dx.doi.org/10.1093/nar/ gkt700
    • (2013) Nucleic Acids Res , vol.41 , pp. 9593-9609
    • Harshman, S.W.1    Young, N.L.2    Parthun, M.R.3    Freitas, M.A.4
  • 12
    • 40549130642 scopus 로고    scopus 로고
    • Cracking the enigmatic linker histone code
    • PMID:18234717
    • Godde JS, Ura K. Cracking the enigmatic linker histone code. J Biochem 2008; 143:287-93; PMID:18234717; http://dx.doi.org/10.1093/jb/ mvn013
    • (2008) J Biochem , vol.143 , pp. 287-293
    • Godde, J.S.1    Ura, K.2
  • 13
    • 0038721220 scopus 로고    scopus 로고
    • H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo
    • PMID:12808097
    • Fan Y, Nikitina T, Morin-Kensicki EM, Zhao J, Magnuson TR, Woodcock CL, Skoultchi AI. H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo. Mol Cell Biol 2003; 23:4559-72; PMID:12808097; http://dx.doi. org/10.1128/MCB.23.13.4559-4572.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 4559-4572
    • Fan, Y.1    Nikitina, T.2    Morin-Kensicki, E.M.3    Zhao, J.4    Magnuson, T.R.5    Woodcock, C.L.6    Skoultchi, A.I.7
  • 14
    • 84884719203 scopus 로고    scopus 로고
    • The embryonic linker histone H1 variant of Drosophila, dBigH1, regulates zygotic genome activation
    • PMID:24055651
    • Pérez-Montero S, Carbonell A, Morán T, Vaquero A, Azorín F. The embryonic linker histone H1 variant of Drosophila, dBigH1, regulates zygotic genome activation. Dev Cell 2013; 26:578-90; PMID:24055651; http://dx.doi.org/10.1016/j. devcel.2013.08.011
    • (2013) Dev Cell , vol.26 , pp. 578-590
    • Pérez-Montero, S.1    Carbonell, A.2    Morán, T.3    Vaquero, A.4    Azorín, F.5
  • 15
    • 70349549948 scopus 로고    scopus 로고
    • Origin and evolution of chromosomal sperm proteins
    • PMID:19708021
    • Eirín-López JM, Ausió J. Origin and evolution of chromosomal sperm proteins. Bioessays 2009; 31:1062-70; PMID:19708021; http://dx.doi. org/10.1002/bies.200900050
    • (2009) Bioessays , vol.31 , pp. 1062-1070
    • Eirín-López, J.M.1    Ausió, J.2
  • 16
    • 0023818350 scopus 로고
    • H 1 histone and histone variants in Trypanosoma cruzi
    • PMID:3121371
    • Toro GC, Galanti N. H 1 histone and histone variants in Trypanosoma cruzi. Exp Cell Res 1988; 174:16-24; PMID:3121371; http://dx.doi. org/10.1016/0014-4827(88)90137-1
    • (1988) Exp Cell Res , vol.174 , pp. 16-24
    • Toro, G.C.1    Galanti, N.2
  • 17
    • 0034766381 scopus 로고    scopus 로고
    • Isolation, characterisation and organisation of histone H1 genes in African trypanosomes
    • PMID:11763441
    • Grüter E, Betschart B. Isolation, characterisation and organisation of histone H1 genes in African trypanosomes. Parasitol Res 2001; 87:977-84; PMID:11763441
    • (2001) Parasitol Res , vol.87 , pp. 977-984
    • Grüter, E.1    Betschart, B.2
  • 18
    • 0014202313 scopus 로고
    • Model nucleoprotein complexes: Studies on the interaction of cationic homopolypeptides with DNA
    • PMID:6030025
    • Olins DE, Olins AL, Von Hippel PH. Model nucleoprotein complexes: studies on the interaction of cationic homopolypeptides with DNA. J Mol Biol 1967; 24:157-76; PMID:6030025; http://dx.doi. org/10.1016/0022-2836(67)90324-5
    • (1967) J Mol Biol , vol.24 , pp. 157-176
    • Olins, D.E.1    Olins, A.L.2    Von Hippel, P.H.3
  • 19
    • 0013959237 scopus 로고
    • The preferential interactions of polylysine and polyarginine with specific base sequences in DNA
    • PMID:5339293
    • Leng M, Felsenfeld G. The preferential interactions of polylysine and polyarginine with specific base sequences in DNA. Proc Natl Acad Sci U S A 1966; 56:1325-32; PMID:5339293; http://dx.doi. org/10.1073/pnas.56.4.1325
    • (1966) Proc Natl Acad Sci U S A , vol.56 , pp. 1325-1332
    • Leng, M.1    Felsenfeld, G.2
  • 20
    • 0023513912 scopus 로고
    • The structure of an oligo(dA). oligo(dT) tract and its biological implications
    • PMID:3670410
    • Nelson HC, Finch JT, Luisi BF, Klug A. The structure of an oligo(dA). oligo(dT) tract and its biological implications. Nature 1987; 330:221-6; PMID:3670410; http://dx.doi. org/10.1038/330221a0
    • (1987) Nature , vol.330 , pp. 221-226
    • Nelson, H.C.1    Finch, J.T.2    Luisi, B.F.3    Klug, A.4
  • 21
    • 60349115060 scopus 로고    scopus 로고
    • Poly(dA:DT) tracts: Major determinants of nucleosome organization
    • PMID:19208466
    • Segal E, Widom J. Poly(dA:dT) tracts: major determinants of nucleosome organization. Curr Opin Struct Biol 2009; 19:65-71; PMID:19208466; http://dx.doi.org/10.1016/j.sbi.2009.01.004
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 65-71
    • Segal, E.1    Widom, J.2
  • 22
    • 0022446807 scopus 로고
    • Roles of H1 domains in determining higher order chromatin structure and H1 location
    • PMID:3458926
    • 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; PMID:3458926; http://dx.doi.org/10.1016/0022-2836(86)90337-2
    • (1986) J Mol Biol , vol.187 , pp. 591-601
    • Allan, J.1    Mitchell, T.2    Harborne, N.3    Bohm, L.4    Crane-Robinson, C.5
  • 23
    • 0025295030 scopus 로고
    • Analysis of the charge distribution in the C-terminal region of histone H1 as related to its interaction with DNA
    • PMID:2361149
    • Subirana JA. Analysis of the charge distribution in the C-terminal region of histone H1 as related to its interaction with DNA. Biopolymers 1990; 29:1351-7; PMID:2361149; http://dx.doi.org/10.1002/ bip.360291003
    • (1990) Biopolymers , vol.29 , pp. 1351-1357
    • Subirana, J.A.1
  • 24
    • 0025327471 scopus 로고
    • Electrostatic mechanism of chromatin folding
    • PMID:2313700
    • Clark DJ, Kimura T. Electrostatic mechanism of chromatin folding. J Mol Biol 1990; 211:883-96; PMID:2313700; http://dx.doi. org/10.1016/0022-2836(90)90081-V
    • (1990) J Mol Biol , vol.211 , pp. 883-896
    • Clark, D.J.1    Kimura, T.2
  • 25
    • 23044489675 scopus 로고    scopus 로고
    • H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain
    • PMID:15911621
    • Th'ng JP, 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; PMID:15911621; http:// dx.doi.org/10.1074/jbc.M501627200
    • (2005) J Biol Chem , vol.280 , pp. 27809-27814
    • Th'ng, J.P.1    Sung, R.2    Ye, M.3    Hendzel, M.J.4
  • 26
    • 58549094957 scopus 로고    scopus 로고
    • Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder
    • PMID:19072710
    • 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; PMID:19072710; http://dx.doi.org/10.1021/bi801636y
    • (2009) Biochemistry , vol.48 , pp. 164-172
    • Lu, X.1    Hamkalo, B.2    Parseghian, M.H.3    Hansen, J.C.4
  • 27
    • 0033850576 scopus 로고    scopus 로고
    • The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: Distribution in human fetal fibroblasts
    • PMID:10997781
    • Parseghian MH, Newcomb RL, Winokur ST, Hamkalo BA. The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: distribution in human fetal fibroblasts. Chromosome Res 2000; 8:405-24; PMID:10997781; http://dx.doi.org/10.1023/A:1009262819961
    • (2000) Chromosome Res , vol.8 , pp. 405-424
    • Parseghian, M.H.1    Newcomb, R.L.2    Winokur, S.T.3    Hamkalo, B.A.4
  • 28
    • 55449090888 scopus 로고    scopus 로고
    • Depletion of human histone H1 variants uncovers specific roles in gene expression and cell growth
    • PMID:18927631
    • 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; PMID:18927631; http://dx.doi. org/10.1371/journal.pgen.1000227
    • (2008) PLoS Genet , vol.4
    • Sancho, M.1    Diani, E.2    Beato, M.3    Jordan, A.4
  • 29
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • PMID:14985337
    • Hendzel MJ, Lever MA, Crawford E, Th'ng JP. The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. J Biol Chem 2004; 279:20028-34; PMID:14985337; http:// dx.doi.org/10.1074/jbc.M400070200
    • (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
  • 30
    • 77950548496 scopus 로고    scopus 로고
    • Dissecting the binding mechanism of the linker histone in live cells: An integrated FRAP analysis
    • PMID:20224551
    • Stasevich TJ, Mueller F, Brown DT, McNally JG. Dissecting the binding mechanism of the linker histone in live cells: an integrated FRAP analysis. EMBO J 2010; 29:1225-34; PMID:20224551; http://dx.doi.org/10.1038/emboj.2010.24
    • (2010) EMBO J , vol.29 , pp. 1225-1234
    • Stasevich, T.J.1    Mueller, F.2    Brown, D.T.3    McNally, J.G.4
  • 31
    • 0028068811 scopus 로고
    • Homoand heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Full assignment, tertiary structure, and comparison with the globular domain of histone H5
    • PMID:7727360
    • Cerf C, Lippens G, Ramakrishnan V, Muyldermans S, Segers A, Wyns L, Wodak SJ, Hallenga K. Homoand heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5. Biochemistry 1994; 33:11079-86; PMID:7727360; http://dx.doi.org/10.1021/ bi00203a004
    • (1994) Biochemistry , vol.33 , pp. 11079-11086
    • Cerf, C.1    Lippens, G.2    Ramakrishnan, V.3    Muyldermans, S.4    Segers, A.5    Wyns, L.6    Wodak, S.J.7    Hallenga, K.8
  • 32
    • 0023355070 scopus 로고
    • The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • PMID:3608994
    • Clore GM, Gronenborn AM, Nilges M, Sukumaran DK, Zarbock J. The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J 1987; 6:1833-42; PMID:3608994
    • (1987) EMBO J , vol.6 , pp. 1833-1842
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Sukumaran, D.K.4    Zarbock, J.5
  • 35
    • 0032563864 scopus 로고    scopus 로고
    • Position and orientation of the globular domain of linker histone H5 on the nucleosome
    • PMID:9759733
    • 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; PMID:9759733; http://dx.doi.org/10.1038/26521
    • (1998) Nature , vol.395 , pp. 402-405
    • Zhou, Y.B.1    Gerchman, S.E.2    Ramakrishnan, V.3    Travers, A.4    Muyldermans, S.5
  • 36
    • 0032972980 scopus 로고    scopus 로고
    • The location of the linker histone on the nucleosome
    • PMID:10087913
    • Travers A. The location of the linker histone on the nucleosome. Trends Biochem Sci 1999; 24:4-7; PMID:10087913; http://dx.doi.org/10.1016/ S0968-0004(98)01339-5
    • (1999) Trends Biochem Sci , vol.24 , pp. 4-7
    • Travers, A.1
  • 38
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin
    • PMID:9826673
    • Bednar J, Horowitz RA, Grigoryev SA, Carruthers LM, Hansen JC, Koster AJ, Woodcock CL. 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 U S A 1998; 95:14173-8; PMID:9826673; http:// dx.doi.org/10.1073/pnas.95.24.14173
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14173-14178
    • Bednar, J.1    Horowitz, R.A.2    Grigoryev, S.A.3    Carruthers, L.M.4    Hansen, J.C.5    Koster, A.J.6    Woodcock, C.L.7
  • 39
    • 0242285999 scopus 로고    scopus 로고
    • Molecular modeling of the chromatosome particle
    • PMID:12853645
    • Bharath MM, Chandra NR, Rao MR. Molecular modeling of the chromatosome particle. Nucleic Acids Res 2003; 31:4264-74; PMID:12853645; http://dx.doi.org/10.1093/nar/gkg481
    • (2003) Nucleic Acids Res , vol.31 , pp. 4264-4274
    • Bharath, M.M.1    Chandra, N.R.2    Rao, M.R.3
  • 40
    • 34250782684 scopus 로고    scopus 로고
    • Extraction, purification and analysis of histones
    • PMID:17545981
    • Shechter D, Dormann HL, Allis CD, Hake SB. Extraction, purification and analysis of histones. Nat Protoc 2007; 2:1445-57; PMID:17545981; http:// dx.doi.org/10.1038/nprot.2007.202
    • (2007) Nat Protoc , vol.2 , pp. 1445-1457
    • Shechter, D.1    Dormann, H.L.2    Allis, C.D.3    Hake, S.B.4
  • 41
    • 73049177682 scopus 로고
    • Further fractionations of histones from calf thymus
    • PMID:14451975
    • Johns EW, Butler JA. Further fractionations of histones from calf thymus. Biochem J 1962; 82:15-8; PMID:14451975
    • (1962) Biochem J , vol.82 , pp. 15-18
    • Johns, E.W.1    Butler, J.A.2
  • 42
    • 0036429193 scopus 로고    scopus 로고
    • The human and mouse replicationdependent histone genes
    • PMID:12408966
    • Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ. The human and mouse replicationdependent histone genes. Genomics 2002; 80:487-98; PMID:12408966; http://dx.doi.org/10.1006/ geno.2002.6850
    • (2002) Genomics , vol.80 , pp. 487-498
    • Marzluff, W.F.1    Gongidi, P.2    Woods, K.R.3    Jin, J.4    Maltais, L.J.5
  • 43
    • 0027238209 scopus 로고
    • Histone H1 deposition and histone-DNA interactions in replicating chromatin
    • PMID:8483911
    • Bavykin S, Srebreva L, Banchev T, Tsanev R, Zlatanova J, Mirzabekov A. Histone H1 deposition and histone-DNA interactions in replicating chromatin. Proc Natl Acad Sci U S A 1993; 90:3918-22; PMID:8483911; http://dx.doi.org/10.1073/ pnas.90.9.3918
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3918-3922
    • Bavykin, S.1    Srebreva, L.2    Banchev, T.3    Tsanev, R.4    Zlatanova, J.5    Mirzabekov, A.6
  • 45
    • 0023711642 scopus 로고
    • Alphahelix in the carboxy-terminal domains of histones H1 and H5
    • PMID:3359996
    • Clark DJ, Hill CS, Martin SR, Thomas JO. Alphahelix in the carboxy-terminal domains of histones H1 and H5. EMBO J 1988; 7:69-75; PMID:3359996
    • (1988) EMBO J , vol.7 , pp. 69-75
    • Clark, D.J.1    Hill, C.S.2    Martin, S.R.3    Thomas, J.O.4
  • 46
    • 0035903114 scopus 로고    scopus 로고
    • Induction of secondary structure in a COOHterminal peptide of histone H1 by interaction with the DNA: An infrared spectroscopy study
    • PMID:11413144
    • Vila R, Ponte I, Collado M, Arrondo JL, Suau P. Induction of secondary structure in a COOHterminal peptide of histone H1 by interaction with the DNA: an infrared spectroscopy study. J Biol Chem 2001; 276:30898-903; PMID:11413144; http://dx.doi.org/10.1074/jbc.M104189200
    • (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
  • 47
    • 25444523218 scopus 로고    scopus 로고
    • DNAinduced secondary structure of the carboxyl-terminal domain of histone H1
    • PMID:16006555
    • Roque A, Iloro I, Ponte I, Arrondo JL, Suau P. DNAinduced secondary structure of the carboxyl-terminal domain of histone H1. J Biol Chem 2005; 280:32141-7; PMID:16006555; http://dx.doi.org/10.1074/jbc. M505636200
    • (2005) J Biol Chem , vol.280 , pp. 32141-32147
    • Roque, A.1    Iloro, I.2    Ponte, I.3    Arrondo, J.L.4    Suau, P.5
  • 48
    • 69549124299 scopus 로고    scopus 로고
    • Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1
    • PMID:19663398
    • 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; PMID:19663398; http://dx.doi.org/10.1021/ jp9022579
    • (2009) J Phys Chem B , vol.113 , pp. 12061-12066
    • Roque, A.1    Ponte, I.2    Suau, P.3
  • 49
    • 79955041234 scopus 로고    scopus 로고
    • Structure of the H1 C-terminal domain and function in chromatin condensation
    • PMID:21326361
    • Caterino TL, Hayes JJ. Structure of the H1 C-terminal domain and function in chromatin condensation. Biochem Cell Biol 2011; 89:35-44; PMID:21326361; http://dx.doi.org/10.1139/O10-024
    • (2011) Biochem Cell Biol , vol.89 , pp. 35-44
    • Caterino, T.L.1    Hayes, J.J.2
  • 50
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • PMID:7479959
    • Arents G, Moudrianakis EN. The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc Natl Acad Sci U S A 1995; 92:11170-4; PMID:7479959; http:// dx.doi.org/10.1073/pnas.92.24.11170
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 51
    • 70349530494 scopus 로고    scopus 로고
    • Long-term evolution of histone families: Old notions and new insights into their diversification mechanisms across eukaryotes
    • In: Pontarotti P, ed. Berlin, Heidelberg: Springer-Verlag
    • Eirín-López JM, González-Romero R, Dryhurst D, Méndez J, Ausió J. Long-term evolution of histone families: old notions and new insights into their diversification mechanisms across eukaryotes. In: Pontarotti P, ed. Evolutionary biology: Concept Modeling, and Application. Berlin, Heidelberg: Springer-Verlag, 2009:139-62.
    • (2009) Evolutionary biology: Concept Modeling, and Application , pp. 139-162
    • Eirín-López, J.M.1    González-Romero, R.2    Dryhurst, D.3    Méndez, J.4    Ausió, J.5
  • 53
    • 0029127222 scopus 로고
    • A variety of DNA-binding and multimeric proteins contain the histone fold motif
    • PMID:7651829
    • Baxevanis AD, Arents G, Moudrianakis EN, Landsman D. A variety of DNA-binding and multimeric proteins contain the histone fold motif. Nucleic Acids Res 1995; 23:2685-91; PMID:7651829; http://dx.doi.org/10.1093/nar/23.14.2685
    • (1995) Nucleic Acids Res , vol.23 , pp. 2685-2691
    • Baxevanis, A.D.1    Arents, G.2    Moudrianakis, E.N.3    Landsman, D.4
  • 54
    • 33748747193 scopus 로고    scopus 로고
    • A unique vertebrate histone H1-related protamine-like protein results in an unusual sperm chromatin organization
    • PMID:16965539
    • Saperas N, Chiva M, Casas MT, Campos JL, Eirín-López JM, Frehlick LJ, Prieto C, Subirana JA, Ausió J. A unique vertebrate histone H1-related protamine-like protein results in an unusual sperm chromatin organization. FEBS J 2006; 273:4548-61; PMID:16965539; http://dx.doi. org/10.1111/j.1742-4658.2006.05461.x
    • (2006) FEBS J , vol.273 , pp. 4548-4561
    • Saperas, N.1    Chiva, M.2    Casas, M.T.3    Campos, J.L.4    Eirín-López, J.M.5    Frehlick, L.J.6    Prieto, C.7    Subirana, J.A.8    Ausió, J.9
  • 55
    • 0027452325 scopus 로고
    • Preferential binding of histone H1 to four-way helical junction DNA
    • PMID:8407888
    • Varga-Weisz P, van Holde K, Zlatanova J. Preferential binding of histone H1 to four-way helical junction DNA. J Biol Chem 1993; 268:20699-700; PMID:8407888
    • (1993) J Biol Chem , vol.268 , pp. 20699-20700
    • Varga-Weisz, P.1    van Holde, K.2    Zlatanova, J.3
  • 56
    • 0024573304 scopus 로고
    • Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome
    • PMID:2716057
    • Ausió J, Dong F, van Holde KE. Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome. J Mol Biol 1989; 206:451-63; PMID:2716057; http://dx.doi. org/10.1016/0022-2836(89)90493-2
    • (1989) J Mol Biol , vol.206 , pp. 451-463
    • Ausió, J.1    Dong, F.2    van Holde, K.E.3
  • 57
    • 33646569673 scopus 로고    scopus 로고
    • Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: Identification of a novel phosphorylation site on histone H1
    • PMID:16377619
    • Sarg B, Helliger W, Talasz H, Förg B, Lindner HH. Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1. J Biol Chem 2006; 281:6573-80; PMID:16377619; http:// dx.doi.org/10.1074/jbc.M508957200
    • (2006) J Biol Chem , vol.281 , pp. 6573-6580
    • Sarg, B.1    Helliger, W.2    Talasz, H.3    Förg, B.4    Lindner, H.H.5
  • 58
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • PMID:17043054
    • Wisniewski JR, Zougman A, Krüger S, 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 2007; 6:72-87; PMID:17043054; http://dx.doi. org/10.1074/mcp.M600255-MCP200
    • (2007) Mol Cell Proteomics , vol.6 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Krüger, S.3    Mann, M.4
  • 59
    • 67650658841 scopus 로고    scopus 로고
    • Post-translational modifications of the linker histone variants and their association with cell mechanisms
    • PMID:19490123
    • 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; PMID:19490123; http://dx.doi. org/10.1111/j.1742-4658.2009.07079.x
    • (2009) FEBS J , vol.276 , pp. 3685-3697
    • Wood, C.1    Snijders, A.2    Williamson, J.3    Reynolds, C.4    Baldwin, J.5    Dickman, M.6
  • 60
    • 79959484677 scopus 로고    scopus 로고
    • Signals and combinatorial functions of histone modifications
    • PMID:21529160
    • Suganuma T, Workman JL. Signals and combinatorial functions of histone modifications. Annu Rev Biochem 2011; 80:473-99; PMID:21529160; http://dx.doi. org/10.1146/annurev-biochem-061809-175347
    • (2011) Annu Rev Biochem , vol.80 , pp. 473-499
    • Suganuma, T.1    Workman, J.L.2
  • 61
    • 49249102932 scopus 로고    scopus 로고
    • Phosphorylation of the carboxy-terminal domain of histone H1: Effects on secondary structure and DNA condensation
    • PMID:18632762
    • Roque A, Ponte I, Arrondo JL, Suau P. Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation. Nucleic Acids Res 2008; 36:4719-26; PMID:18632762; http://dx.doi.org/10.1093/nar/ gkn440
    • (2008) Nucleic Acids Res , vol.36 , pp. 4719-4726
    • Roque, A.1    Ponte, I.2    Arrondo, J.L.3    Suau, P.4
  • 62
    • 59149103350 scopus 로고    scopus 로고
    • M phase-specific phosphorylation of histone H1.5 at threonine 10 by GSK-3
    • PMID:19136008
    • Happel N, Stoldt S, Schmidt B, Doenecke D. M phase-specific phosphorylation of histone H1.5 at threonine 10 by GSK-3. J Mol Biol 2009; 386:339-50; PMID:19136008; http://dx.doi.org/10.1016/j. jmb.2008.12.047
    • (2009) J Mol Biol , vol.386 , pp. 339-350
    • Happel, N.1    Stoldt, S.2    Schmidt, B.3    Doenecke, D.4
  • 63
    • 0031835671 scopus 로고    scopus 로고
    • Linker histone tails and N-tails of histone H3 are redundant: Scanning force microscopy studies of reconstituted fibers
    • PMID:9635737
    • Leuba SH, Bustamante C, van Holde K, Zlatanova J. Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers. Biophys J 1998; 74:2830-9; PMID:9635737; http://dx.doi.org/10.1016/ S0006-3495(98)77990-1
    • (1998) Biophys J , vol.74 , pp. 2830-2839
    • Leuba, S.H.1    Bustamante, C.2    van Holde, K.3    Zlatanova, J.4
  • 64
    • 0033975839 scopus 로고    scopus 로고
    • Histone H1 is a specific repressor of core histone acetylation in chromatin
    • PMID:10611231
    • Herrera JE, West KL, Schiltz RL, Nakatani Y, Bustin M. Histone H1 is a specific repressor of core histone acetylation in chromatin. Mol Cell Biol 2000; 20:523-9; PMID:10611231; http://dx.doi. org/10.1128/MCB.20.2.523-529.2000
    • (2000) Mol Cell Biol , vol.20 , pp. 523-529
    • Herrera, J.E.1    West, K.L.2    Schiltz, R.L.3    Nakatani, Y.4    Bustin, M.5
  • 65
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • PMID:11130728
    • Lever MA, Th'ng JP, Sun X, Hendzel MJ. Rapid exchange of histone H1.1 on chromatin in living human cells. Nature 2000; 408:873-6; PMID:11130728; http://dx.doi.org/10.1038/35048603
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 66
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • PMID:11130729
    • Misteli T, Gunjan A, Hock R, Bustin M, Brown DT. Dynamic binding of histone H1 to chromatin in living cells. Nature 2000; 408:877-81; PMID:11130729; http://dx.doi.org/10.1038/35048610
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 67
    • 0019880525 scopus 로고
    • Exchange of histone H1 between segments of chromatin
    • PMID:7277492
    • Caron F, Thomas JO. Exchange of histone H1 between segments of chromatin. J Mol Biol 1981; 146:513-37; PMID:7277492; http://dx.doi. org/10.1016/0022-2836(81)90045-0
    • (1981) J Mol Biol , vol.146 , pp. 513-537
    • Caron, F.1    Thomas, J.O.2
  • 68
    • 2942733480 scopus 로고    scopus 로고
    • PL-I of Spisula solidissima, a highly elongated sperm-specific histone H1
    • PMID:15196019
    • Lewis JD, McParland R, Ausió J. PL-I of Spisula solidissima, a highly elongated sperm-specific histone H1. Biochemistry 2004; 43:7766-75; PMID:15196019; http://dx.doi.org/10.1021/ bi0360455
    • (2004) Biochemistry , vol.43 , pp. 7766-7775
    • Lewis, J.D.1    McParland, R.2    Ausió, J.3
  • 69
    • 0024100359 scopus 로고
    • Expression of a histone H1-like protein is restricted to early Xenopus development
    • PMID:3060404
    • Smith RC, Dworkin-Rastl E, Dworkin MB. Expression of a histone H1-like protein is restricted to early Xenopus development. Genes Dev 1988; 2:1284-95; PMID:3060404; http://dx.doi.org/10.1101/ gad.2.10.1284
    • (1988) Genes Dev , vol.2 , pp. 1284-1295
    • Smith, R.C.1    Dworkin-Rastl, E.2    Dworkin, M.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.