메뉴 건너뛰기




Volumn 74, Issue 6, 1998, Pages 2823-2829

Contributions of linker histones and histone H3 to chromatin structure: Scanning force microscopy studies on trypsinized fibers

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HISTONE H3;

EID: 0031806540     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77989-5     Document Type: Article
Times cited : (61)

References (42)
  • 1
    • 0020131558 scopus 로고
    • Participation of core histone "tails" in the stabilization of the chromatin solenoid
    • Allan, J., N. Harborne, D. C. Rau, and H. Gould. 1982. Participation of core histone "tails" in the stabilization of the chromatin solenoid. J. Cell Biol. 93:285-297.
    • (1982) J. Cell Biol. , vol.93 , pp. 285-297
    • Allan, J.1    Harborne, N.2    Rau, D.C.3    Gould, H.4
  • 2
    • 0019157001 scopus 로고
    • The structure of histone H1 and its location in chromatin
    • Allan, J., P. G. Hartman, C. Crane-Robinson, and F. X. Aviles. 1980. The structure of histone H1 and its location in chromatin. Nature. 288: 675-679.
    • (1980) Nature , vol.288 , pp. 675-679
    • Allan, J.1    Hartman, P.G.2    Crane-Robinson, C.3    Aviles, F.X.4
  • 4
    • 0021266689 scopus 로고
    • Proteases as structural probes for chromatin: The domain structure of histones
    • Böhm, L., and C. Crane-Robinson. 1984. Proteases as structural probes for chromatin: the domain structure of histones. Biosci. Rep. 4:365-386.
    • (1984) Biosci. Rep. , vol.4 , pp. 365-386
    • Böhm, L.1    Crane-Robinson, C.2
  • 5
    • 0018866555 scopus 로고
    • Points of contact between histone H1 and the histone octamer
    • Boulikas, T., J. M. Wiseman, and W. T. Garrard. 1980. Points of contact between histone H1 and the histone octamer. Proc. Natl. Acad. Sci. USA. 77:127-131.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 127-131
    • Boulikas, T.1    Wiseman, J.M.2    Garrard, W.T.3
  • 6
    • 0028077880 scopus 로고
    • Biochemical and structural applications of scanning force microscopy
    • Bustamante, C., D. A. Erie, and D. Keller. 1994. Biochemical and structural applications of scanning force microscopy. Curr. Opin. Struct. Biol. 4:750-760.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 750-760
    • Bustamante, C.1    Erie, D.A.2    Keller, D.3
  • 7
    • 11944275288 scopus 로고
    • Scanning force microscopy in biology
    • Bustamante, C., and D. Keller. 1995. Scanning force microscopy in biology. Phys. Today. 48:32-38.
    • (1995) Phys. Today , vol.48 , pp. 32-38
    • Bustamante, C.1    Keller, D.2
  • 8
    • 0027274701 scopus 로고
    • Scanning force microscopy of nucleic acids and nucleoprotein assemblies
    • Bustamante, C., D. Keller, and G. Yang. 1993. Scanning force microscopy of nucleic acids and nucleoprotein assemblies. Curr. Opin. Struct. Biol. 3:363-372.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 363-372
    • Bustamante, C.1    Keller, D.2    Yang, G.3
  • 9
    • 0015912240 scopus 로고
    • The modification of deoxyribonucleohistone by trypsin and chymotrypsin
    • Chatterjee, S., and I. O. Walker. 1973. The modification of deoxyribonucleohistone by trypsin and chymotrypsin. Eur. J. Biochem. 34:519-526.
    • (1973) Eur. J. Biochem. , vol.34 , pp. 519-526
    • Chatterjee, S.1    Walker, I.O.2
  • 10
    • 0019452561 scopus 로고
    • The electron microscopic appearance of soluble rat liver chromatin mounted on different supports
    • De Murcia, G., and T. Koller. 1981. The electron microscopic appearance of soluble rat liver chromatin mounted on different supports. Biol. Cell. 40:165-174.
    • (1981) Biol. Cell , vol.40 , pp. 165-174
    • De Murcia, G.1    Koller, T.2
  • 11
    • 0028858566 scopus 로고
    • Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms
    • Fletcher, T. M., and J. C. Hansen. 1995. Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms. J. Biol. Chem. 270:25359-25362.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25359-25362
    • Fletcher, T.M.1    Hansen, J.C.2
  • 12
    • 0026782131 scopus 로고
    • Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1
    • Garcia-Ramirez, M., F. Dong, and J. Ausio. 1992. Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1. J. Biol. Chem. 267:19587-19595.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19587-19595
    • Garcia-Ramirez, M.1    Dong, F.2    Ausio, J.3
  • 13
    • 21144470639 scopus 로고
    • Tip-sample forces in scanning probe microscopy in air and vacuum
    • Grigg, D. A., P. E. Russell, and J. E. Griffith. 1992. Tip-sample forces in scanning probe microscopy in air and vacuum. J. Vac. Sci. Technol. A. 10:680-683.
    • (1992) J. Vac. Sci. Technol. A , vol.10 , pp. 680-683
    • Grigg, D.A.1    Russell, P.E.2    Griffith, J.E.3
  • 14
    • 0025605331 scopus 로고
    • Accessibility and structural role of histone domains in chromatin. Biophysical and immunochemical studies of progressive digestion with immobilized proteases
    • Hacques, M.-F., S. Muller, G. De Murcia, M. H. V. Van Regenmortel, and C. Marion. 1990. Accessibility and structural role of histone domains in chromatin. Biophysical and immunochemical studies of progressive digestion with immobilized proteases. J. Biomol. Struct. Dyn. 8:619-641.
    • (1990) J. Biomol. Struct. Dyn. , vol.8 , pp. 619-641
    • Hacques, M.-F.1    Muller, S.2    De Murcia, G.3    Van Regenmortel, M.H.V.4    Marion, C.5
  • 15
    • 0028221098 scopus 로고
    • The three-dimensional architecture of chromatin in situ: Electron tomography reveals fibers composed of a continuously variable zig-zag nucleosomal ribbon
    • Horowitz, R. A., D. A. Agard, J. W. Sedat, and C. L. Woodcock. 1994. The three-dimensional architecture of chromatin in situ: electron tomography reveals fibers composed of a continuously variable zig-zag nucleosomal ribbon. J. Cell. Biol. 125:1-10.
    • (1994) J. Cell. Biol. , vol.125 , pp. 1-10
    • Horowitz, R.A.1    Agard, D.A.2    Sedat, J.W.3    Woodcock, C.L.4
  • 16
    • 0000986826 scopus 로고
    • Imaging the condensation and evaporation of molecularly thin films of water with nanometer resolution
    • Hu, J., X.-D. Xiao, D. F. Olgetree, and M. Salmeron. 1995. Imaging the condensation and evaporation of molecularly thin films of water with nanometer resolution. Science. 268:267-269.
    • (1995) Science , vol.268 , pp. 267-269
    • Hu, J.1    Xiao, X.-D.2    Olgetree, D.F.3    Salmeron, M.4
  • 17
    • 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
  • 18
  • 19
    • 0027414475 scopus 로고
    • On the location of histones H1 and H5 in the chromatin fiber. Studies with immobilized trypsin and chymotrypsin
    • Leuba, S. H., J. Zlatanova, and K. van Holde. 1993. On the location of histones H1 and H5 in the chromatin fiber. Studies with immobilized trypsin and chymotrypsin. J. Mol. Biol. 229:917-929.
    • (1993) J. Mol. Biol. , vol.229 , pp. 917-929
    • Leuba, S.H.1    Zlatanova, J.2    Van Holde, K.3
  • 20
    • 0028047760 scopus 로고
    • On the location of linker DNA in the chromatin fiber. Studies with immobilized and soluble micrococcal nuclease
    • Leuba, S. H., J. Zlatanova, and K. van Holde. 1994b. On the location of linker DNA in the chromatin fiber. Studies with immobilized and soluble micrococcal nuclease. J. Mol. Biol. 235:871-880.
    • (1994) J. Mol. Biol. , vol.235 , pp. 871-880
    • Leuba, S.H.1    Zlatanova, J.2    Van Holde, K.3
  • 21
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., A. W. Mäder, R. K. Richmond, D. F. Sargent, and T. J. Richmond. 1997. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature. 389:250-260.
    • (1997) Nature , vol.389 , pp. 250-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 22
    • 0021765518 scopus 로고
    • The role of histone H1 and non-structured domains of core histones in maintaining the orientation of nucleosomes within the chromatin fiber
    • Makarov, V. L., S. I. Dimitrov, I. R. Tsaneva, and I. G. Pashev. 1984. The role of histone H1 and non-structured domains of core histones in maintaining the orientation of nucleosomes within the chromatin fiber. Biochem. Biophys. Res. Commun. 122:1021-1027.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1021-1027
    • Makarov, V.L.1    Dimitrov, S.I.2    Tsaneva, I.R.3    Pashev, I.G.4
  • 23
    • 0021094812 scopus 로고
    • Role of histones H1 and H3 in the maintenance of chromatin in a compact conformation
    • Marion, C., B. Roux, and P. R. Coulet. 1983a. Role of histones H1 and H3 in the maintenance of chromatin in a compact conformation. FEBS Lett. 157:317-321.
    • (1983) FEBS Lett. , vol.157 , pp. 317-321
    • Marion, C.1    Roux, B.2    Coulet, P.R.3
  • 24
    • 0021101731 scopus 로고
    • Study of chromatin organization with trypsin immobilized on collagen membranes
    • Marion, C., B. Roux, L. Pallotta, and P. R. Coulet. 1983b. Study of chromatin organization with trypsin immobilized on collagen membranes. Biochem. Biophys. Res. Commun. 114:1169-1175.
    • (1983) Biochem. Biophys. Res. Commun. , vol.114 , pp. 1169-1175
    • Marion, C.1    Roux, B.2    Pallotta, L.3    Coulet, P.R.4
  • 25
    • 0021760689 scopus 로고
    • Structure of the nucleosomal core particle at 7 Åresolution
    • Richmond, T. J., J. T. Finch, B. Rushton, D. Rhodes, and A. Klug. 1984. Structure of the nucleosomal core particle at 7 Åresolution. Nature. 311:532-537.
    • (1984) Nature , vol.311 , pp. 532-537
    • Richmond, T.J.1    Finch, J.T.2    Rushton, B.3    Rhodes, D.4    Klug, A.5
  • 26
    • 0023406952 scopus 로고
    • Accessibility of the globular domain of histones H1 and H5 to antibodies upon folding of chromatin
    • Russanova, V. R., S. I. Dimitrov, V. L. Makarov, and I. G. Pashev. 1987. Accessibility of the globular domain of histones H1 and H5 to antibodies upon folding of chromatin. Eur. J. Biochem. 167:321-326.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 321-326
    • Russanova, V.R.1    Dimitrov, S.I.2    Makarov, V.L.3    Pashev, I.G.4
  • 27
    • 0020628385 scopus 로고
    • Resistance of chromatin superstructure to trypsin digestion modulated by conjugated polyacrylamide
    • Saccone, G. T. P., J. D. Skinner, and L. A. Burgoyne. 1983. Resistance of chromatin superstructure to trypsin digestion modulated by conjugated polyacrylamide. FEBS Lett. 157:111-114.
    • (1983) FEBS Lett. , vol.157 , pp. 111-114
    • Saccone, G.T.P.1    Skinner, J.D.2    Burgoyne, L.A.3
  • 28
    • 0029882454 scopus 로고    scopus 로고
    • Reversible oligonucleosome self-association: Dependence on divalent cations and core histone tail domains
    • Schwarz, P. M., A. Felthauser, T. M. Fletcher, and J. C. Hansen. 1996. Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry. 35:4009-4015.
    • (1996) Biochemistry , vol.35 , pp. 4009-4015
    • Schwarz, P.M.1    Felthauser, A.2    Fletcher, T.M.3    Hansen, J.C.4
  • 29
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma, F., T. Koller, and A. Klug. 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
  • 31
    • 0003903126 scopus 로고
    • Springer Verlag, New York
    • van Holde, K. E. 1988. Chromatin. Springer Verlag, New York.
    • (1988) Chromatin
    • Van Holde, K.E.1
  • 32
    • 0028935863 scopus 로고
    • Chromatin higher order structure: Chasing a mirage?
    • van Holde, K., and J. Zlatanova. 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.1    Zlatanova, J.2
  • 33
    • 0029780079 scopus 로고    scopus 로고
    • What determines the folding of the chromatin fiber?
    • van Holde, K., and J. Zlatanova. 1996. What determines the folding of the chromatin fiber? Proc. Natl. Acad. Sci. USA. 93:10548-10555.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10548-10555
    • Van Holde, K.1    Zlatanova, J.2
  • 35
    • 0002666194 scopus 로고
    • Dissection of chromosome structure with trypsin and nucleases
    • Weintraub, H., and F. van Lente. 1974. Dissection of chromosome structure with trypsin and nucleases. Proc. Natl. Acad. Sci. USA. 71: 4249-4253.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4249-4253
    • Weintraub, H.1    Van Lente, F.2
  • 36
    • 0027517831 scopus 로고
    • A chromatin folding model that incorporates linker variability generates fibers resembling the native structures
    • Woodcock, C. L., S. A. Grigoryev, R. A. Horowitz, and N. Whitaker. 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
  • 38
    • 0024537375 scopus 로고
    • Salt-induced release of DNA from nucleosome core particles
    • Yager, T. D., C. T. McMurray, and K. E. van Holde. 1989. Salt-induced release of DNA from nucleosome core particles. Biochemistry. 28: 2271-2281.
    • (1989) Biochemistry , vol.28 , pp. 2271-2281
    • Yager, T.D.1    McMurray, C.T.2    Van Holde, K.E.3
  • 40
    • 0029225431 scopus 로고
    • Role of the structural domains of the linker histones and histone H3 in the chromatin fiber structure at low ionic strength: SFM studies on partially trypsinized chromatin
    • Zlatanova, J., S. H. Leuba, C. Bustamante, and K. van Holde. 1995. Role of the structural domains of the linker histones and histone H3 in the chromatin fiber structure at low ionic strength: SFM studies on partially trypsinized chromatin. SPIE. 2384:22-32.
    • (1995) SPIE , vol.2384 , pp. 22-32
    • Zlatanova, J.1    Leuba, S.H.2    Bustamante, C.3    Van Holde, K.4
  • 41
    • 0031968760 scopus 로고    scopus 로고
    • Chromatin fiber structure: Morphology, molecular determinants, structural transitions
    • in press
    • Zlatanova, J., S. H. Leuba, and K. van Holde. 1998. Chromatin fiber structure: morphology, molecular determinants, structural transitions. Biophys. J. (in press).
    • (1998) Biophys. J.
    • Zlatanova, J.1    Leuba, S.H.2    Van Holde, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.