메뉴 건너뛰기




Volumn 22, Issue 1, 2008, Pages 316-326

H2A.Bbd: A quickly evolving hypervariable mammalian histone that destabilizes nucleosomes in an acetylation-independent way

Author keywords

Chromatin; Evolution; Sedimentation velocity

Indexed keywords

HISTONE H2A; NUCLEOPROTEIN; HISTONE;

EID: 38049153427     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-9255com     Document Type: Article
Times cited : (41)

References (57)
  • 1
    • 0003903126 scopus 로고
    • Springer-Verlag, New York
    • Van Holde, K. E. (1988) Chromatin. Springer-Verlag, New York
    • (1988) Chromatin
    • Van Holde, K.E.1
  • 3
    • 36148973603 scopus 로고    scopus 로고
    • The role of histone variability in chromatin stability and folding
    • Zlatanova, J, and Leuba, S. H, eds pp, Elsevier, New York
    • Ausió, J., and Abbott, D. W. (2004) The role of histone variability in chromatin stability and folding. In Chromatin Structure and Dynamics: State-of-the-Art (Zlatanova, J., and Leuba, S. H., eds) pp. 241-290, Elsevier, New York
    • (2004) Chromatin Structure and Dynamics: State-of-the-Art , pp. 241-290
    • Ausió, J.1    Abbott, D.W.2
  • 4
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson, C. L., and Laniel, M. A. (2004) Histones and histone modifications. Curr. Biol. 14, R546-R551
    • (2004) Curr. Biol , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 5
    • 33947496350 scopus 로고    scopus 로고
    • Epigenetic regulators and histone modification
    • Imhof, A. (2006) Epigenetic regulators and histone modification. Brief. Funct. Genomic. Proteomic. 5, 222-227
    • (2006) Brief. Funct. Genomic. Proteomic , vol.5 , pp. 222-227
    • Imhof, A.1
  • 6
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function. Cell 128, 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 7
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B., and Allis, C. D. (2000) The language of covalent histone modifications. Nature 403, 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.1    Allis, C.D.2
  • 9
    • 33947524604 scopus 로고    scopus 로고
    • Histone variants - the structure behind the function
    • Ausio, J. (2006) Histone variants - the structure behind the function. Brief. Funct. Genomic. Proteomic. 5, 228-243
    • (2006) Brief. Funct. Genomic. Proteomic , vol.5 , pp. 228-243
    • Ausio, J.1
  • 10
    • 0035931749 scopus 로고    scopus 로고
    • A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
    • Chadwick, B. P., and Willard, H. F. (2001) A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. J. Cell Biol. 152, 375-384
    • (2001) J. Cell Biol , vol.152 , pp. 375-384
    • Chadwick, B.P.1    Willard, H.F.2
  • 11
    • 0035336967 scopus 로고    scopus 로고
    • Histone H2A variants and the inactive X chromosome: Identification of a second macroH2A variant
    • Chadwick, B. P., and Willard, H. F. (2001) Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant. Hum. Mol. Genet. 10, 1101-1113
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1101-1113
    • Chadwick, B.P.1    Willard, H.F.2
  • 12
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large nonhistone region
    • Pehrson, J. R., and Fried, V. A. (1992) MacroH2A, a core histone containing a large nonhistone region. Science 257, 1398-1400
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 13
  • 16
    • 27944478598 scopus 로고    scopus 로고
    • Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I
    • Okuwaki, M., Kato, K., Shimahara, H., Tate, S. I., and Nagata, K. (2005) Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I. Mol. Cell. Biol. 25, 10639-10651
    • (2005) Mol. Cell. Biol , vol.25 , pp. 10639-10651
    • Okuwaki, M.1    Kato, K.2    Shimahara, H.3    Tate, S.I.4    Nagata, K.5
  • 17
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • Malik, H. S., and Henikoff, S. (2003) Phylogenomics of the nucleosome. Nat. Struct. Biol. 10, 882-891
    • (2003) Nat. Struct. Biol , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 18
    • 38149116549 scopus 로고    scopus 로고
    • Hall, T. A. (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Ser. 41, 95-98
    • Hall, T. A. (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Ser. 41, 95-98
  • 19
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar, S., Tamura, K., and Nei, M. (2004) MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5, 150-163
    • (2004) Brief. Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 20
    • 30344446662 scopus 로고    scopus 로고
    • LogoBar: Bar graph visualization of protein logos with gaps
    • Perez-Bercoff, A., Koch, J., and Burglin, T. R. (2006) LogoBar: bar graph visualization of protein logos with gaps. Bioinformatics 22, 112-114
    • (2006) Bioinformatics , vol.22 , pp. 112-114
    • Perez-Bercoff, A.1    Koch, J.2    Burglin, T.R.3
  • 22
    • 0032584099 scopus 로고    scopus 로고
    • Positive Darwinian selection after gene duplication in primate ribonuclease genes
    • Zhang, J., Rosenberg, H. F., and Nei, M. (1998) Positive Darwinian selection after gene duplication in primate ribonuclease genes. Proc. Natl. Acad. Sci. U. S. A. 95, 3708-3713
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 3708-3713
    • Zhang, J.1    Rosenberg, H.F.2    Nei, M.3
  • 23
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and Nei, M. (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406-425
    • (1987) Mol. Biol. Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 24
    • 0026660413 scopus 로고
    • A simple method for estimating and testing minimum-evolution trees
    • Rzhetsky, A., and Nei, M. (1992) A simple method for estimating and testing minimum-evolution trees. Mol. Biol. Evol. 9, 945-967
    • (1992) Mol. Biol. Evol , vol.9 , pp. 945-967
    • Rzhetsky, A.1    Nei, M.2
  • 25
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsestein, J. (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution Int. J. Org. Evolution 39, 783-791
    • (1985) Evolution Int. J. Org. Evolution , vol.39 , pp. 783-791
    • Felsestein, J.1
  • 26
    • 0029965168 scopus 로고    scopus 로고
    • Bootstrap method of interior-branch test for phylogenetic trees
    • Sitnikova, T. (1996) Bootstrap method of interior-branch test for phylogenetic trees. Mol. Biol. Evol. 13, 605-611
    • (1996) Mol. Biol. Evol , vol.13 , pp. 605-611
    • Sitnikova, T.1
  • 27
    • 0028985519 scopus 로고
    • Interior-branch and bootstrap tests of phylogenetic trees
    • Sitnikova, T., Rzhetsky, A., and Nei, M. (1995) Interior-branch and bootstrap tests of phylogenetic trees. Mol. Biol. Evol. 12, 319-333
    • (1995) Mol. Biol. Evol , vol.12 , pp. 319-333
    • Sitnikova, T.1    Rzhetsky, A.2    Nei, M.3
  • 28
    • 33745107476 scopus 로고    scopus 로고
    • Frehlick, L. J., Eirin-Lopez, J. M., Jeffery, E. D., Hunt, D. F., and Ausio, J. (2006) The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling. BMC Genomics 7, 99 [Published online April 28, 2006. doi: 10.1186/1471-2164-7-99]
    • Frehlick, L. J., Eirin-Lopez, J. M., Jeffery, E. D., Hunt, D. F., and Ausio, J. (2006) The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling. BMC Genomics 7, 99 [Published online April 28, 2006. doi: 10.1186/1471-2164-7-99]
  • 29
    • 0024573304 scopus 로고
    • Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome
    • Ausió, J., Dong, F., and van Holde, K. E. (1989) Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome. J. Molec. Biol. 206, 451-463
    • (1989) J. Molec. Biol , vol.206 , pp. 451-463
    • Ausió, J.1    Dong, F.2    van Holde, K.E.3
  • 30
    • 0034634558 scopus 로고    scopus 로고
    • Acetylation increases the alpha-helical content of the histone tails of the nucleosome
    • Wang, X., Moore, S. C., Laszckzak, M., and Ausió, J. (2000) Acetylation increases the alpha-helical content of the histone tails of the nucleosome. J. Biol. Chem. 275, 35,013-35,020
    • (2000) J. Biol. Chem , vol.275
    • Wang, X.1    Moore, S.C.2    Laszckzak, M.3    Ausió, J.4
  • 31
    • 0018802021 scopus 로고
    • Nucleosome reconstitution: Effect of DNA length on nucleosome structure
    • Thatchell, K., and van Holde, K. E. (1979) Nucleosome reconstitution: effect of DNA length on nucleosome structure. Biochemistry 18, 2871-2880
    • (1979) Biochemistry , vol.18 , pp. 2871-2880
    • Thatchell, K.1    van Holde, K.E.2
  • 32
    • 0031669634 scopus 로고    scopus 로고
    • Reconstitution of chromatin complexes from high-performance liquid chromatography-purified histones
    • Ausió, J., and Moore, S. C. (1998) Reconstitution of chromatin complexes from high-performance liquid chromatography-purified histones. Methods 15, 333-342
    • (1998) Methods , vol.15 , pp. 333-342
    • Ausió, J.1    Moore, S.C.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 14044274310 scopus 로고    scopus 로고
    • Li, A., Maffey, A. H., Abbott, D. W., Conde e Silva, N., Prunell, A., Siino, J., Churikov, D., Zalensky, A. O., and Ausió, J. (2005) Characterization of nucleosomes consisting of the human testis/sperm-specific histone H2B variant (hTSH2B). Biochemistry 44, 2529-2535
    • Li, A., Maffey, A. H., Abbott, D. W., Conde e Silva, N., Prunell, A., Siino, J., Churikov, D., Zalensky, A. O., and Ausió, J. (2005) Characterization of nucleosomes consisting of the human testis/sperm-specific histone H2B variant (hTSH2B). Biochemistry 44, 2529-2535
  • 36
    • 0021352605 scopus 로고
    • Dynamics and equilibria of nucleosomes at elevated ionic strength
    • Yager, T. D., and van Holde, K. E. (1984) Dynamics and equilibria of nucleosomes at elevated ionic strength. J. Biol. Chem. 259, 4212-4222
    • (1984) J. Biol. Chem , vol.259 , pp. 4212-4222
    • Yager, T.D.1    van Holde, K.E.2
  • 37
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • Arents, G., and Moudrianakis, E. N. (1995) The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc. Natl. Acad. Sci. U. S. A. 92, 11170-11174
    • (1995) Proc. Natl. Acad. Sci. U. S. A , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 38
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389, 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 40
    • 27744485938 scopus 로고    scopus 로고
    • H2AX: Tailoring histone H2A for chromatin-dependent genomic integrity
    • Li, A., Eirín-López, J. M., and Ausió, J. (2005) H2AX: tailoring histone H2A for chromatin-dependent genomic integrity. Biochem. Cell Biol. 83, 505-515
    • (2005) Biochem. Cell Biol , vol.83 , pp. 505-515
    • Li, A.1    Eirín-López, J.M.2    Ausió, J.3
  • 41
    • 33745851176 scopus 로고    scopus 로고
    • The X and Y chromosomes assemble into H2A.Z-containing facultative heterochromatin following meiosis
    • Greaves, I. K., Rangasamy, D., Devoy, M., Marshall Graves, J. A., and Tremethick, D. J. (2006) The X and Y chromosomes assemble into H2A.Z-containing facultative heterochromatin following meiosis. Mol. Cell. Biol. 26, 5394-5405
    • (2006) Mol. Cell. Biol , vol.26 , pp. 5394-5405
    • Greaves, I.K.1    Rangasamy, D.2    Devoy, M.3    Marshall Graves, J.A.4    Tremethick, D.J.5
  • 42
    • 0022551060 scopus 로고
    • Histone hyperacetylation: Its effects on nucleosome conformation and stability
    • Ausió, J., and van Holde, K. E. (1986) Histone hyperacetylation: its effects on nucleosome conformation and stability. Biochemistry. 25, 1421-1428
    • (1986) Biochemistry , vol.25 , pp. 1421-1428
    • Ausió, J.1    van Holde, K.E.2
  • 43
    • 0020479282 scopus 로고
    • Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation
    • Perry, M., and Chalkley, R. (1982) Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation. J. Biol. Chem. 257, 7336-7347
    • (1982) J. Biol. Chem , vol.257 , pp. 7336-7347
    • Perry, M.1    Chalkley, R.2
  • 44
    • 38149037462 scopus 로고
    • Part A, Academic Press, New York
    • Isenberg, I. (1978) Histones, Vol. 4, Part A, Academic Press, New York
    • (1978) Histones , vol.4
    • Isenberg, I.1
  • 45
    • 0038718585 scopus 로고    scopus 로고
    • A walk though vertebrate and invertebrate protamines
    • Lewis, J. D., Song, Y., de Jong, M., Bagha, S., and Ausió, J. (2003) A walk though vertebrate and invertebrate protamines. Chromosoma 111, 473-482
    • (2003) Chromosoma , vol.111 , pp. 473-482
    • Lewis, J.D.1    Song, Y.2    de Jong, M.3    Bagha, S.4    Ausió, J.5
  • 46
    • 0027146049 scopus 로고
    • Evolution of proprotamine P2 genes in primates
    • Retief, J. D., and Dixon, G. H. (1993) Evolution of proprotamine P2 genes in primates. Eur. J. Biochem. 218, 1095
    • (1993) Eur. J. Biochem , vol.218 , pp. 1095
    • Retief, J.D.1    Dixon, G.H.2
  • 47
    • 0032931263 scopus 로고    scopus 로고
    • Rapid evolution of a primate sperm protein: Relaxation of functional constraint or positive Darwinian selection?
    • Rooney, A. P., and Zhang, J. (1999) Rapid evolution of a primate sperm protein: relaxation of functional constraint or positive Darwinian selection? Mol. Biol. Evol. 16, 706-710
    • (1999) Mol. Biol. Evol , vol.16 , pp. 706-710
    • Rooney, A.P.1    Zhang, J.2
  • 48
    • 0034688140 scopus 로고    scopus 로고
    • Rapid evolution of male reproductive genes in the descent of man
    • Wyckoff, G. J., Wang, W., and Wu, C. I. (2000) Rapid evolution of male reproductive genes in the descent of man. Nature 403, 304-309
    • (2000) Nature , vol.403 , pp. 304-309
    • Wyckoff, G.J.1    Wang, W.2    Wu, C.I.3
  • 49
    • 4944233486 scopus 로고    scopus 로고
    • Eirín-López, J. M., González-Tizón, A. M., Martínez, A., and Méndez, J. (2004) Birth-and-death evolution with strong purifying selection in the histone H1 multigene family and the origin of orphon H1 genes. Mol. Biol. Evol. 21, 1992-2003
    • Eirín-López, J. M., González-Tizón, A. M., Martínez, A., and Méndez, J. (2004) Birth-and-death evolution with strong purifying selection in the histone H1 multigene family and the origin of orphon H1 genes. Mol. Biol. Evol. 21, 1992-2003
  • 50
    • 1542267778 scopus 로고    scopus 로고
    • Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome
    • Levchenko, V., and Jackson, V. (2004) Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome. Biochemistry 43, 2359-2352
    • (2004) Biochemistry , vol.43 , pp. 2359-2352
    • Levchenko, V.1    Jackson, V.2
  • 51
    • 33750732646 scopus 로고    scopus 로고
    • Long-range histone acetylation: Biological significance, structural implications, and mechanisms
    • Calestagne-Morelli, A., and Ausio, J. (2006) Long-range histone acetylation: biological significance, structural implications, and mechanisms. Biochem. Cell Biol. 84, 518-527
    • (2006) Biochem. Cell Biol , vol.84 , pp. 518-527
    • Calestagne-Morelli, A.1    Ausio, J.2
  • 52
    • 0029046603 scopus 로고
    • Modulation of chromatin folding by histone acetylation
    • Garcia-Ramirez, M., Rocchini, C., and Ausio, J. (1995) Modulation of chromatin folding by histone acetylation. J. Biol. Chem. 270, 17923-17928
    • (1995) J. Biol. Chem , vol.270 , pp. 17923-17928
    • Garcia-Ramirez, M.1    Rocchini, C.2    Ausio, J.3
  • 53
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • Norton, V. G., Imai, B. S., Yau, P., and Bradbury, E. M. (1989) Histone acetylation reduces nucleosome core particle linking number change. Cell 57, 449-457
    • (1989) Cell , vol.57 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 54
    • 33746457753 scopus 로고    scopus 로고
    • Enhanced histone acetylation and transcription: A dynamic perspective
    • Clayton, A. L., Hazzalin, C. A., and Mahadevan, L. C. (2006) Enhanced histone acetylation and transcription: a dynamic perspective. Mol. Cell 23, 289-296
    • (2006) Mol. Cell , vol.23 , pp. 289-296
    • Clayton, A.L.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 55
  • 56
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: Requirements for the histone H4 N-terminal tail
    • Dorigo, B., Schalch, T., Bystricky, K., and Richmond, T. J. (2003) Chromatin fiber folding: requirements for the histone H4 N-terminal tail. J. Mol. Biol. 327, 85-96
    • (2003) J. Mol. Biol , vol.327 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.