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Volumn 26, Issue 6, 2007, Pages 445-452

Effect of salt on the binding of the linker histone HI to DNA and nucleosomes

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DNA; DNA; HISTONE H1; MAGNESIUM CHLORIDE; SODIUM CHLORIDE;

EID: 34250899779     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/dna.2006.0512     Document Type: Article
Times cited : (6)

References (21)
  • 2
    • 0026430080 scopus 로고
    • Purification of histone H10 and its subfractions under non-denaturing conditions
    • BANCHEV, T., SREBREVA, L., and ZLATANOVA, J. (1991). Purification of histone H10 and its subfractions under non-denaturing conditions. Biochim. Biophys. Acta. 1073, 230-232.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 230-232
    • BANCHEV, T.1    SREBREVA, L.2    ZLATANOVA, J.3
  • 3
    • 0028049305 scopus 로고
    • The twist, writhe and overall shape of supercoiled DNA change during counterion-induced transition from a loosely to a tightly interwound superhelix. Possible implications for DNA structure in vivo
    • BEDNAR, J., FURRER, P., STASIAK, A., DUBOCHET, J., EGELMAN, E.H., and BATES, A.D. (1994). The twist, writhe and overall shape of supercoiled DNA change during counterion-induced transition from a loosely to a tightly interwound superhelix. Possible implications for DNA structure in vivo. J. Mol. Biol. 235, 825-847.
    • (1994) J. Mol. Biol , vol.235 , pp. 825-847
    • BEDNAR, J.1    FURRER, P.2    STASIAK, A.3    DUBOCHET, J.4    EGELMAN, E.H.5    BATES, A.D.6
  • 4
    • 0017133394 scopus 로고
    • The organization of histones and DNA in chromatin: Evidence for an arginine-rich histone kernel
    • CAMERINI-OTERO, R.D., SOLLNER-WEBB, B., and FELSENFELD, G. (1976). The organization of histones and DNA in chromatin: evidence for an arginine-rich histone kernel. Cell 8, 333-347.
    • (1976) Cell , vol.8 , pp. 333-347
    • CAMERINI-OTERO, R.D.1    SOLLNER-WEBB, B.2    FELSENFELD, G.3
  • 5
    • 0022470051 scopus 로고
    • Salt-dependent co-operative interaction of histone H1 with linear DNA
    • CLARK, D.J., and THOMAS, J.O. (1986). Salt-dependent co-operative interaction of histone H1 with linear DNA. J. Mol. Biol. 187, 569-580.
    • (1986) J. Mol. Biol , vol.187 , pp. 569-580
    • CLARK, D.J.1    THOMAS, J.O.2
  • 6
    • 0022517271 scopus 로고
    • Formation and characterization of soluble complexes of histone H1 with supercoiled DNA
    • DE BERNARDIN, W., LOSA, R., and KOLLER, T. (1986). Formation and characterization of soluble complexes of histone H1 with supercoiled DNA. J. Mol. Biol. 189, 503-517.
    • (1986) J. Mol. Biol , vol.189 , pp. 503-517
    • DE BERNARDIN, W.1    LOSA, R.2    KOLLER, T.3
  • 7
    • 2942748432 scopus 로고    scopus 로고
    • Linker histone interaction shows divalent character with both supercoiled and linear DNA
    • ELLEN, T.P., and VAN HOLDE, K.E. (2004). Linker histone interaction shows divalent character with both supercoiled and linear DNA. Biochemistry 43, 7867-7872.
    • (2004) Biochemistry , vol.43 , pp. 7867-7872
    • ELLEN, T.P.1    VAN HOLDE, K.E.2
  • 8
    • 0035937419 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes stabilize SWI/SNF binding to promoter nucleosomes
    • HASSAN, A.H., NEELY, K.E., and WORKMAN, J.L. (2001). Histone acetyltransferase complexes stabilize SWI/SNF binding to promoter nucleosomes. Cell 104, 817-827.
    • (2001) Cell , vol.104 , pp. 817-827
    • HASSAN, A.H.1    NEELY, K.E.2    WORKMAN, J.L.3
  • 9
    • 25444436189 scopus 로고    scopus 로고
    • Linker histone H1 per se can induce three-dimensional folding of chromatin fiber
    • HIZUME, K., YOSHIMURA, S.H., and TAKEYASU, K. (2005). Linker histone H1 per se can induce three-dimensional folding of chromatin fiber. Biochemistry 44, 12978-12989.
    • (2005) Biochemistry , vol.44 , pp. 12978-12989
    • HIZUME, K.1    YOSHIMURA, S.H.2    TAKEYASU, K.3
  • 10
    • 0031037411 scopus 로고    scopus 로고
    • Deoxyribonuclease I-facilitated electrotransfer of protein-DNA complexes from electrophoretic gels to nitrocellulose membranes
    • IVANCHENKO, M., and ZLATANOVA, J. (1997). Deoxyribonuclease I-facilitated electrotransfer of protein-DNA complexes from electrophoretic gels to nitrocellulose membranes. Electrophoresis 18, 72-73.
    • (1997) Electrophoresis , vol.18 , pp. 72-73
    • IVANCHENKO, M.1    ZLATANOVA, J.2
  • 11
    • 0031047889 scopus 로고    scopus 로고
    • Histone H1 preferentially binds to superhelical DNA molecules of higher compaction
    • IVANCHENKO, M., ZLATANOVA, J., and VAN HOLDE, K.E. (1997). Histone H1 preferentially binds to superhelical DNA molecules of higher compaction. Biophys. J. 72, 1388-1395.
    • (1997) Biophys. J , vol.72 , pp. 1388-1395
    • IVANCHENKO, M.1    ZLATANOVA, J.2    VAN HOLDE, K.E.3
  • 12
    • 0028559510 scopus 로고
    • Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini
    • JUAN, L.J., UTLEY, R.T., ADAMS, C.C., VETTESE-DADEY, M., and WORKMAN, J.L. (1994). Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini. EMBO J. 13, 6031-6040.
    • (1994) EMBO J , vol.13 , pp. 6031-6040
    • JUAN, L.J.1    UTLEY, R.T.2    ADAMS, C.C.3    VETTESE-DADEY, M.4    WORKMAN, J.L.5
  • 14
    • 0027961109 scopus 로고
    • The influence of salt on the structure and energetics of supercoiled DNA
    • SCHLICK, T., LI, B., and OLSON, W.K. (1994). The influence of salt on the structure and energetics of supercoiled DNA. Biophys. J. 67, 2146-2166.
    • (1994) Biophys. J , vol.67 , pp. 2146-2166
    • SCHLICK, T.1    LI, B.2    OLSON, W.K.3
  • 15
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • THOMA, F., KOLLER, T., and KLUG, A. (1979). Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J. Cell Biol. 83, 403-427.
    • (1979) J. Cell Biol , vol.83 , pp. 403-427
    • THOMA, F.1    KOLLER, T.2    KLUG, A.3
  • 16
    • 0019268071 scopus 로고
    • Cross-linking of histone H1 in chromatin
    • THOMAS, J.O., and KHABAZA, A.J.A. (1980). Cross-linking of histone H1 in chromatin. Eur. J. Biochem. 112, 501-511.
    • (1980) Eur. J. Biochem , vol.112 , pp. 501-511
    • THOMAS, J.O.1    KHABAZA, A.J.A.2
  • 17
    • 0026597552 scopus 로고
    • Cooperative binding of the globular domains of histones H1 and H5 to DNA
    • THOMAS, J.O., REES, C., and FINCH, J.T. (1992). Cooperative binding of the globular domains of histones H1 and H5 to DNA. Nucleic Acids Res. 20, 187-194.
    • (1992) Nucleic Acids Res , vol.20 , pp. 187-194
    • THOMAS, J.O.1    REES, C.2    FINCH, J.T.3
  • 18
    • 0003903126 scopus 로고
    • Springer-Verlag, New York
    • VAN HOLDE, K.E. (1989). Chromatin. (Springer-Verlag, New York).
    • (1989) Chromatin
    • VAN HOLDE, K.E.1
  • 21
    • 0023056623 scopus 로고
    • Cooperative interaction of histone H1 with DNA
    • WATANABE, F. (1986). Cooperative interaction of histone H1 with DNA. Nucleic Acids Res. 14, 3573-3785.
    • (1986) Nucleic Acids Res , vol.14 , pp. 3573-3785
    • WATANABE, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.