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Volumn 30, Issue 23, 2002, Pages 5103-5109

Circle ligation of in vitro assembled chromatin indicates a highly flexible structure

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA FRAGMENT; EXODEOXYRIBONUCLEASE III; HISTONE; MAGNESIUM; NAKED DNA; PLASMID DNA; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; POLYGLUTAMIC ACID; SODIUM CHLORIDE;

EID: 0036920409     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkf671     Document Type: Review
Times cited : (17)

References (33)
  • 2
    • 0029051646 scopus 로고
    • Transcription complex stability and chromatin dynamics in vivo
    • Wijgerde,M., Grosveld,F. and Fraser,P. (1995) Transcription complex stability and chromatin dynamics in vivo. Nature, 377, 209-213.
    • (1995) Nature , vol.377 , pp. 209-213
    • Wijgerde, M.1    Grosveld, F.2    Fraser, P.3
  • 3
    • 0030960672 scopus 로고    scopus 로고
    • Transcriptional activation by recruitment
    • Ptashne,M. and Gann,A. (1997) Transcriptional activation by recruitment. Nature, 386, 569-577.
    • (1997) Nature , vol.386 , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 4
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch,J.T. and Klug,A. (1976) Solenoidal model for superstructure in chromatin. Proc. Natl Acad. Sci. USA, 73, 1897-1901.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 1897-1901
    • Finch, J.T.1    Klug, A.2
  • 5
    • 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.H. 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.H.2    Klug, A.3
  • 6
    • 0027517831 scopus 로고
    • A chromatin folding model that incorporates linker variability generates fibers resembling the native structures
    • Woodcock,C.L., Grigoryev,S.A., Horowitz,R.A. and Whitaker,N. (1993) A chromatin folding model that incorporates linker variability generates fibers resembling the native structures. Proc. Natl Acad. Sci. USA, 90, 9021-9025.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9021-9025
    • Woodcock, C.L.1    Grigoryev, S.A.2    Horowitz, R.A.3    Whitaker, N.4
  • 7
    • 0028286015 scopus 로고
    • Linker DNA accessibility in chromatin fibers of different conformations: A reevaluation
    • Zlatanova,J., Leuba,S.H., Yang,G., Bustamante,C. and van Holde,K. (1994) Linker DNA accessibility in chromatin fibers of different conformations: a reevaluation. Proc. Natl Acad. Sci. USA, 91, 5277-5280.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5277-5280
    • Zlatanova, J.1    Leuba, S.H.2    Yang, G.3    Bustamante, C.4    van Holde, K.5
  • 8
  • 9
    • 0028935863 scopus 로고
    • Chromatin higher order structure: Chasing a mirage?
    • van Holde,K.E. and Zlatanova,J. (1995) Chromatin higher order structure: chasing a mirage? J. Biol. Chem., 270, 8373-8376.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8373-8376
    • van Holde, K.E.1    Zlatanova, J.2
  • 10
    • 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
  • 11
    • 0033485539 scopus 로고    scopus 로고
    • Quantitative comparison of DNA looping in vitro and in vivo: Chromatin increases effective DNA flexibility at short distances
    • Ringrose,L., Chabanis,S., Angrand,P., Woodroofe,C. and Stewart,A.F. (1999) Quantitative comparison of DNA looping in vitro and in vivo: chromatin increases effective DNA flexibility at short distances. EMBO J., 18, 6630-6641.
    • (1999) EMBO J. , vol.18 , pp. 6630-6641
    • Ringrose, L.1    Chabanis, S.2    Angrand, P.3    Woodroofe, C.4    Stewart, A.F.5
  • 12
    • 0026355279 scopus 로고
    • Chromatin assembly on plasmid DNA in vitro: Apparent spreading of nucleosome alignment from one region of pBR327 by histone H5
    • Jeong,S., Lauderdale,J.D. and Stein,A. (1991) Chromatin assembly on plasmid DNA in vitro: apparent spreading of nucleosome alignment from one region of pBR327 by histone H5. J. Mol. Biol., 222, 1131-1147.
    • (1991) J. Mol. Biol. , vol.222 , pp. 1131-1147
    • Jeong, S.1    Lauderdale, J.D.2    Stein, A.3
  • 13
    • 0027058511 scopus 로고
    • Introns of the chicken ovalbumin gene promote nucleosome alignment in vitro
    • Lauderdale,J.D. and Stein,A. (1992) Introns of the chicken ovalbumin gene promote nucleosome alignment in vitro. Nucleic Acids Res., 20, 6589-6596.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6589-6596
    • Lauderdale, J.D.1    Stein, A.2
  • 14
    • 0031586220 scopus 로고    scopus 로고
    • DNA sequence encodes information for nucleosome array formation
    • Liu,K. and Stein,A. (1997) DNA sequence encodes information for nucleosome array formation. J. Mol. Biol., 270, 559-573.
    • (1997) J. Mol. Biol. , vol.270 , pp. 559-573
    • Liu, K.1    Stein, A.2
  • 15
    • 0033081336 scopus 로고    scopus 로고
    • A signal encoded in vertebrate DNA that influences nucleosome positioning and alignment
    • Stein,A. and Bina,M. (1999) A signal encoded in vertebrate DNA that influences nucleosome positioning and alignment. Nucleic Acids Res., 27, 848-853.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 848-853
    • Stein, A.1    Bina, M.2
  • 16
    • 0028363760 scopus 로고
    • Formation and stability of higher order chromatin structures
    • Schwarz,P.M. and Hansen,J.C. (1994) Formation and stability of higher order chromatin structures. J. Biol. Chem., 269, 16284-16289.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16284-16289
    • Schwarz, P.M.1    Hansen, J.C.2
  • 17
    • 0021590954 scopus 로고
    • A model chromatin assembly system: Factors affecting nucleosome spacing
    • Stein,A. and Bina,M. (1984) A model chromatin assembly system: factors affecting nucleosome spacing. J. Mol. Biol., 178, 341-363.
    • (1984) J. Mol. Biol. , vol.178 , pp. 341-363
    • Stein, A.1    Bina, M.2
  • 19
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned fragments and core histones: A model system for study of higher order structure
    • Simpson,R.T., Thoma,F. and Brubaker,J.M. (1985) Chromatin reconstituted from tandemly repeated cloned fragments and core histones: A model system for study of higher order structure. Cell, 42, 799-808.
    • (1985) Cell , vol.42 , pp. 799-808
    • Simpson, R.T.1    Thoma, F.2    Brubaker, J.M.3
  • 20
    • 0000684866 scopus 로고
    • Energetics of B to Z transition in DNA
    • Peck,L.J. and Wang,J.C. (1983) Energetics of B to Z transition in DNA. Proc. Natl Acad. Sci. USA, 80, 6206-6210.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 6206-6210
    • Peck, L.J.1    Wang, J.C.2
  • 21
    • 0020478940 scopus 로고
    • Nucleosome spacing in rat liver chromatin. A study with exonuclease III
    • Strauss,F. and Prunell,A. (1982) Nucleosome spacing in rat liver chromatin. A study with exonuclease III. Nucleic Acids Res., 10, 2275-2293.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 2275-2293
    • Strauss, F.1    Prunell, A.2
  • 22
    • 0017806223 scopus 로고
    • Boundary analysis of sedimentation-velocity experiments with monodisperse and paucidisperse solutes
    • van Holde,K.E. and Weischet,W.O. (1978) Boundary analysis of sedimentation-velocity experiments with monodisperse and paucidisperse solutes. Biopolymers, 17, 1387-1403.
    • (1978) Biopolymers , vol.17 , pp. 1387-1403
    • van Holde, K.E.1    Weischet, W.O.2
  • 23
    • 0019130753 scopus 로고
    • Changes in chromatin folding in solution
    • Butler,P.J.G. and Thomas,J.O. (1980) Changes in chromatin folding in solution. J. Mol. Biol., 140, 505-529.
    • (1980) J. Mol. Biol. , vol.140 , pp. 505-529
    • Butler, P.J.G.1    Thomas, J.O.2
  • 24
    • 0003751509 scopus 로고
    • W.H.Freeman and Co., San Francisco
    • Cantor,C.R. and Schimmel,P.R. (1980) Biophysical Chemistry, part II. W.H.Freeman and Co., San Francisco, pp. 560-561.
    • (1980) Biophysical Chemistry , Issue.PART II , pp. 560-561
    • Cantor, C.R.1    Schimmel, P.R.2
  • 25
    • 0022544946 scopus 로고
    • Physicochemical studies of the folding of the 100Å nucleosome filament into the 300Å filament
    • Widom,J. (1986) Physicochemical studies of the folding of the 100Å nucleosome filament into the 300Å filament. Cation dependence. J. Mol. Biol., 190, 411-424.
    • (1986) Cation Dependence. J. Mol. Biol. , vol.190 , pp. 411-424
    • Widom, J.1
  • 26
    • 3843114319 scopus 로고
    • Intramolecular reaction in polycondensations, I: The theory of linear systems
    • Jacobson,H. and Stockmayer,W.H. (1950) Intramolecular reaction in polycondensations, I: the theory of linear systems. J. Chem. Phys., 18, 1600-1606.
    • (1950) J. Chem. Phys. , vol.18 , pp. 1600-1606
    • Jacobson, H.1    Stockmayer, W.H.2
  • 27
    • 36849102256 scopus 로고
    • Statistical mechanics of wormlike chains. II. Excluded volume effects
    • Yamakawa,H. and Stockmayer,W.H. (1972) Statistical mechanics of wormlike chains. II. Excluded volume effects. J. Chem. Phys., 57, 2843-2854.
    • (1972) J. Chem. Phys. , vol.57 , pp. 2843-2854
    • Yamakawa, H.1    Stockmayer, W.H.2
  • 28
    • 0000545475 scopus 로고
    • Ring closure probabilities for twisted wormlike chains: Application to DNA
    • Shimada,J. and Yamakawa,H. (1984) Ring closure probabilities for twisted wormlike chains: application to DNA. Macromolecules, 17, 689-698.
    • (1984) Macromolecules , vol.17 , pp. 689-698
    • Shimada, J.1    Yamakawa, H.2
  • 29
    • 0001191247 scopus 로고
    • DNA flexibility studied by covalent closure of short fragments into circles
    • Shore,D., Langowski,J. and Baldwin,R.L. (1981) DNA flexibility studied by covalent closure of short fragments into circles. Proc. Natl Acad. Sci. USA, 78, 4833-4837.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4833-4837
    • Shore, D.1    Langowski, J.2    Baldwin, R.L.3
  • 30
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding
    • Carruthers,L.M., Bednar,J., Woodcock,C.L. and Hansen,J.C. (1998) Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding. Biochemistry, 37, 14776-14787.
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.L.3    Hansen, J.C.4
  • 31
    • 0023663417 scopus 로고
    • Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones
    • Lorch,Y., La Pointe,J.W. and Kornberg,R.D. (1987) Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones. Cell, 49, 203-210.
    • (1987) Cell , vol.49 , pp. 203-210
    • Lorch, Y.1    La Pointe, J.W.2    Kornberg, R.D.3
  • 32
    • 0018363156 scopus 로고
    • DNA folding by histones: The kinetics of chromatin core particle assembly and the interaction of nucleosomes with histones
    • Stein,A. (1979) DNA folding by histones: the kinetics of chromatin core particle assembly and the interaction of nucleosomes with histones. J. Mol. Biol., 130, 103-134.
    • (1979) J. Mol. Biol. , vol.130 , pp. 103-134
    • Stein, A.1
  • 33
    • 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
    • Bednar,J. Horowitz,R.A., Grigoryev,S.A., Carruthers,L.M., Hansen,J.C., Koster,A.J. and Woodcock,C.L. (1998) 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, 95, 14173-14178.
    • (1998) Proc. Natl Acad. Sci. USA , 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


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