메뉴 건너뛰기




Volumn 7, Issue 3, 1997, Pages 362-366

Visualizing nucleic acids and their complexes using electron microscopy

Author keywords

[No Author keywords available]

Indexed keywords

CURVED DNA; DNA; NUCLEIC ACID; PROTEIN; RNA;

EID: 0031011592     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80052-8     Document Type: Article
Times cited : (15)

References (42)
  • 1
    • 0343446730 scopus 로고
    • Griffith J.D. New York: John Wiley and Sons
    • Griffith JD. Electron Microscopy in Biology. II:1982;John Wiley and Sons, New York.
    • (1982) Electron Microscopy in Biology , vol.2
  • 2
    • 0017869441 scopus 로고
    • Electron microscopic visualization of chromatin and other DNA - protein complexes
    • Griffith J, Christiansen G. Electron microscopic visualization of chromatin and other DNA - protein complexes. Annu Rev Biophys Bioeng. 7:1978;19-35.
    • (1978) Annu Rev Biophys Bioeng , vol.7 , pp. 19-35
    • Griffith, J.1    Christiansen, G.2
  • 3
    • 0026666265 scopus 로고
    • Electron microscopic visualization of DNA and DNA - protein complexes as adjunct to biochemical studies
    • Thresher R, Griffith J. Electron microscopic visualization of DNA and DNA - protein complexes as adjunct to biochemical studies. Methods Enzymol. 211:1992;481-490.
    • (1992) Methods Enzymol , vol.211 , pp. 481-490
    • Thresher, R.1    Griffith, J.2
  • 4
    • 0343011045 scopus 로고
    • A general method for labelling specific ends of DNA with biotin, biotin - streptavadin, or radioactive nucleotides
    • Bortner C, Griffith J. A general method for labelling specific ends of DNA with biotin, biotin - streptavadin, or radioactive nucleotides. US Biochem Comm. 20:1993;1-5.
    • (1993) US Biochem Comm , vol.20 , pp. 1-5
    • Bortner, C.1    Griffith, J.2
  • 5
    • 0025355750 scopus 로고
    • Electron microscopy mapping of pBR322 DNA curvature. Comparison with theoretical models
    • Muzard G, Theveny B, Revet B. Electron microscopy mapping of pBR322 DNA curvature. Comparison with theoretical models. EMBO J. 9:1990;1289-1298.
    • (1990) EMBO J , vol.9 , pp. 1289-1298
    • Muzard, G.1    Theveny, B.2    Revet, B.3
  • 7
    • 0029583420 scopus 로고
    • Chromatin conformation and salt-induced compaction: Three-dimensional structural information from cryoelectron microscopy
    • Bednar J, Horowitz RA, DuBochet J, Woodcock CL. Chromatin conformation and salt-induced compaction: three-dimensional structural information from cryoelectron microscopy. J Cell Biol. 131:1995;1365-1376.
    • (1995) J Cell Biol , vol.131 , pp. 1365-1376
    • Bednar, J.1    Horowitz, R.A.2    Dubochet, J.3    Woodcock, C.L.4
  • 8
    • 0029007043 scopus 로고
    • Fate of linear and supercoiled multinucleosomic templates during transcription
    • This work describes a convincing EM approach to a problem that has been unusually difficult to solve biochemically. of outstanding interest
    • Heggeler-Bordier BT, Schild-Poulter C, Chapel S, Wahli W. Fate of linear and supercoiled multinucleosomic templates during transcription. EMBO J. 14:1995;2561-2569 This work describes a convincing EM approach to a problem that has been unusually difficult to solve biochemically. of outstanding interest.
    • (1995) EMBO J , vol.14 , pp. 2561-2569
    • Heggeler-Bordier, B.T.1    Schild-Poulter, C.2    Chapel, S.3    Wahli, W.4
  • 9
    • 0027941198 scopus 로고
    • Preferential nucleosome assembly at DNA triplet repeats from the myotonic dystrophy gene
    • Wang Y-H, Amirhaeri S, Kang S, Wells RD, Griffith J. Preferential nucleosome assembly at DNA triplet repeats from the myotonic dystrophy gene. Science. 265:1994;669-671.
    • (1994) Science , vol.265 , pp. 669-671
    • Wang, Y.-H.1    Amirhaeri, S.2    Kang, S.3    Wells, R.D.4    Griffith, J.5
  • 10
    • 0030575839 scopus 로고    scopus 로고
    • Long CCG triplet repeat blocks exclude nucleosomes: A possible mechanism for the nature of fragile sites in chromosomes
    • This paper together with [8], provides a excellent example of how direct EM visualization can provide important insights into problems of importance in medical genetics. of outstanding interest
    • Wang Y-H, Gellibolian R, Shimizu M, Wells RD, Griffith J. Long CCG triplet repeat blocks exclude nucleosomes: a possible mechanism for the nature of fragile sites in chromosomes. J Mol Biol. 263:1996;511-516 This paper together with [8], provides a excellent example of how direct EM visualization can provide important insights into problems of importance in medical genetics. of outstanding interest.
    • (1996) J Mol Biol , vol.263 , pp. 511-516
    • Wang, Y.-H.1    Gellibolian, R.2    Shimizu, M.3    Wells, R.D.4    Griffith, J.5
  • 11
    • 0029100264 scopus 로고
    • Relative orientation of RNA helices in a group I ribozyme determined by helix extension electron microscopy
    • The description of helix extension microscopy and of its use to study fine structure of a complex, folded RNA. of outstanding interest
    • Nakamura T, Wang Y-H, Zaug A, Griffith J, Cech T. Relative orientation of RNA helices in a group I ribozyme determined by helix extension electron microscopy. EMBO J. 14:1995;4849-4859 The description of helix extension microscopy and of its use to study fine structure of a complex, folded RNA. of outstanding interest.
    • (1995) EMBO J , vol.14 , pp. 4849-4859
    • Nakamura, T.1    Wang, Y.-H.2    Zaug, A.3    Griffith, J.4    Cech, T.5
  • 12
    • 0030985675 scopus 로고    scopus 로고
    • Human p53 binds Holliday junctions strongly and facilitates their cleavage
    • Lee S, Cavallo L, Griffith J. Human p53 binds Holliday junctions strongly and facilitates their cleavage. J Biol Chem. 272:1997;7532-7539.
    • (1997) J Biol Chem , vol.272 , pp. 7532-7539
    • Lee, S.1    Cavallo, L.2    Griffith, J.3
  • 13
    • 0031051010 scopus 로고    scopus 로고
    • Saccharomyces cerevissiae MSH2, a mispaired base recognition protein also recognizes Holliday junctions in DNA
    • Alani E, Lee S, Kane M, Griffith J, Kolodner R. Saccharomyces cerevissiae MSH2, a mispaired base recognition protein also recognizes Holliday junctions in DNA. J Mol Biol. 265:1997;289-301.
    • (1997) J Mol Biol , vol.265 , pp. 289-301
    • Alani, E.1    Lee, S.2    Kane, M.3    Griffith, J.4    Kolodner, R.5
  • 14
    • 0027260602 scopus 로고
    • Imaging of RNA - protein interactions in splicing complexes with dark-field STEM
    • Sibbald MJ, Carlemalm EC, Beer M, Sproat BS. Imaging of RNA - protein interactions in splicing complexes with dark-field STEM. J Struct Biol. 110:1993;111-121.
    • (1993) J Struct Biol , vol.110 , pp. 111-121
    • Sibbald, M.J.1    Carlemalm, E.C.2    Beer, M.3    Sproat, B.S.4
  • 15
    • 0029983584 scopus 로고    scopus 로고
    • Structure of recombinant rat UBF by electron image analysis and homology modelling
    • An excellent application of STEM analysis and molecular modeling. of outstanding interest
    • Neil KJ, Ridsdale RA, Rutherford B, Taylor L, Larson DE, Glibetic M, Rothblum LI, Harauz G. Structure of recombinant rat UBF by electron image analysis and homology modelling. Nucleic Acids Res. 24:1996;1472-1480 An excellent application of STEM analysis and molecular modeling. of outstanding interest.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1472-1480
    • Neil, K.J.1    Ridsdale, R.A.2    Rutherford, B.3    Taylor, L.4    Larson, D.E.5    Glibetic, M.6    Rothblum, L.I.7    Harauz, G.8
  • 16
    • 0029150031 scopus 로고
    • TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a toroid-shaped molecule that binds transcripts containing GAG or UAG repeats separated by two nucleotides
    • Babitzke P, Bear DG, Yanofsky C. TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a toroid-shaped molecule that binds transcripts containing GAG or UAG repeats separated by two nucleotides. Proc Natl Acad Sci USA. 92:1995;7916-7920.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7916-7920
    • Babitzke, P.1    Bear, D.G.2    Yanofsky, C.3
  • 17
    • 0029759341 scopus 로고    scopus 로고
    • Single-stranded DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase
    • Blackwell LJ, Borowiec JA, Mastrangelo IA. Single-stranded DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase. Mol Cell Biol. 16:1996;4798-4807.
    • (1996) Mol Cell Biol , vol.16 , pp. 4798-4807
    • Blackwell, L.J.1    Borowiec, J.A.2    Mastrangelo, I.A.3
  • 18
    • 0023058994 scopus 로고
    • Visualization of the bent helix in kinetoplast DNA by electron microscopy
    • Griffith J, Bleyman M, Rauch C, Kitchin P, Englund P. Visualization of the bent helix in kinetoplast DNA by electron microscopy. Cell. 46:1986;717-724.
    • (1986) Cell , vol.46 , pp. 717-724
    • Griffith, J.1    Bleyman, M.2    Rauch, C.3    Kitchin, P.4    Englund, P.5
  • 19
    • 0028956314 scopus 로고
    • Visualization of TBP oligomers binding and bending the HIV-1 and adeno promoters
    • This work presents several EM approaches to measuring DNA bending. of outstanding interest
    • Griffith J, Makhov A, Zawel L, Reinberg D. Visualization of TBP oligomers binding and bending the HIV-1 and adeno promoters. J Mol Biol. 246:1995;576-584 This work presents several EM approaches to measuring DNA bending. of outstanding interest.
    • (1995) J Mol Biol , vol.246 , pp. 576-584
    • Griffith, J.1    Makhov, A.2    Zawel, L.3    Reinberg, D.4
  • 20
    • 0026654184 scopus 로고
    • An electron microscopic study of (A)BC excinuclease: DNA is sharply bent in the UVRB - DNA complex
    • Shi Q, Thresher R, Sancar A, Griffith J. An electron microscopic study of (A)BC excinuclease: DNA is sharply bent in the UVRB - DNA complex. J Mol Biol. 226:1992;425-432.
    • (1992) J Mol Biol , vol.226 , pp. 425-432
    • Shi, Q.1    Thresher, R.2    Sancar, A.3    Griffith, J.4
  • 21
    • 0027968833 scopus 로고
    • Flow linear dichroism and electron microscopic analysis of protein - DNA complexes of a mutant UvrB protein that binds to but cannot kink DNA
    • Hsu D, Takahashi M, Delagoutte E, Bertrand-Burrgraf E, Wang Y-H, Norden B, Fuchs R, Griffith J, Sancar A. Flow linear dichroism and electron microscopic analysis of protein - DNA complexes of a mutant UvrB protein that binds to but cannot kink DNA. J Mol Biol. 241:1994;645-650.
    • (1994) J Mol Biol , vol.241 , pp. 645-650
    • Hsu, D.1    Takahashi, M.2    Delagoutte, E.3    Bertrand-Burrgraf, E.4    Wang, Y.-H.5    Norden, B.6    Fuchs, R.7    Griffith, J.8    Sancar, A.9
  • 22
    • 0022545056 scopus 로고
    • DNA loops induced by cooperative binding of lambda repressor
    • Griffith J, Hochschild A, Ptashne M. DNA loops induced by cooperative binding of lambda repressor. Nature. 322:1986;750-752.
    • (1986) Nature , vol.322 , pp. 750-752
    • Griffith, J.1    Hochschild, A.2    Ptashne, M.3
  • 25
    • 0025836660 scopus 로고
    • Epstein - Barr nuclear antigen 1 mediates a DNA loop within the latent replication origin of Epstein - Barr virus
    • Frappier L, O'Donnell M. Epstein - Barr nuclear antigen 1 mediates a DNA loop within the latent replication origin of Epstein - Barr virus. Proc Natl Acad Sci USA. 88:1991;10875-10879.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10875-10879
    • Frappier, L.1    O'Donnell, M.2
  • 26
    • 0025721021 scopus 로고
    • DNA looping between the origin of replication of Epstein - Barr virus and its enhancer site: Stabilization of an origin complex with Epstein - Barr nuclear antigen 1
    • Su W, Middleton T, Sugden B, Echols H. DNA looping between the origin of replication of Epstein - Barr virus and its enhancer site: stabilization of an origin complex with Epstein - Barr nuclear antigen 1. Proc Natl Acad Sci USA. 88:1991;10870-10874.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10870-10874
    • Su, W.1    Middleton, T.2    Sugden, B.3    Echols, H.4
  • 27
    • 0027170306 scopus 로고
    • RIP60 dimers and multiples of dimers assemble link structures at an origin of bidirectional replication in the dihydrofolate reductase amplicon of chinese hamster ovary cells
    • Mastrangelo IA, Held PG, Dailey L, Wall JS, Hough PVC, Heintz N, Heintz NH. RIP60 dimers and multiples of dimers assemble link structures at an origin of bidirectional replication in the dihydrofolate reductase amplicon of chinese hamster ovary cells. J Mol Biol. 232:1993;766-778.
    • (1993) J Mol Biol , vol.232 , pp. 766-778
    • Mastrangelo, I.A.1    Held, P.G.2    Dailey, L.3    Wall, J.S.4    Hough, P.V.C.5    Heintz, N.6    Heintz, N.H.7
  • 28
    • 0029923754 scopus 로고    scopus 로고
    • The herpes simplex virus type I UL9 protein carries out origin specific DNA unwinding and forms stem/loop structures
    • This study describes the ATP-dependent growth of DNA loops and several means of its analysis using EM. of special interest
    • Makhov A, Boehmer P, Lehman IR, Griffith J. The herpes simplex virus type I UL9 protein carries out origin specific DNA unwinding and forms stem/loop structures. EMBO J. 15:1996;1742-1750 This study describes the ATP-dependent growth of DNA loops and several means of its analysis using EM. of special interest.
    • (1996) EMBO J , vol.15 , pp. 1742-1750
    • Makhov, A.1    Boehmer, P.2    Lehman, I.R.3    Griffith, J.4
  • 29
    • 0028330508 scopus 로고
    • Visualization of protein - nucleic acid interactions involved in the in vitro assembly of the Escherichia coli 50 S ribosomal subunit
    • Tumminia SJ, Hellmann W, Wall JS, Boublik M. Visualization of protein - nucleic acid interactions involved in the in vitro assembly of the Escherichia coli 50 S ribosomal subunit. J Mol Biol. 235:1994;1239-1250.
    • (1994) J Mol Biol , vol.235 , pp. 1239-1250
    • Tumminia, S.J.1    Hellmann, W.2    Wall, J.S.3    Boublik, M.4
  • 30
    • 0029989329 scopus 로고    scopus 로고
    • Mass spectrometric composition and molecular mass of Lumbricus terrestris hemoglobin: A refined model of its quaternary structure
    • Martin PD, Kuchumov AR, Green BN, Oliver RWA, Braswell EH, Wall JS, Vinogradov SN. Mass spectrometric composition and molecular mass of Lumbricus terrestris hemoglobin: a refined model of its quaternary structure. J Mol Biol. 255:1996;154-169.
    • (1996) J Mol Biol , vol.255 , pp. 154-169
    • Martin, P.D.1    Kuchumov, A.R.2    Green, B.N.3    Oliver, R.W.A.4    Braswell, E.H.5    Wall, J.S.6    Vinogradov, S.N.7
  • 31
    • 0021095633 scopus 로고
    • Procedure for freeze-drying molecules adsorbed to mica flakes
    • Heuser J. Procedure for freeze-drying molecules adsorbed to mica flakes. J Mol Biol. 169:1983;155-195.
    • (1983) J Mol Biol , vol.169 , pp. 155-195
    • Heuser, J.1
  • 32
    • 0024843435 scopus 로고
    • Visualization of RecA protein and its complexes with DNA by quick-freeze/deep-etch electron microscopy
    • Heuser J, Griffith J. Visualization of RecA protein and its complexes with DNA by quick-freeze/deep-etch electron microscopy. J Mol Biol. 210:1989;473-484.
    • (1989) J Mol Biol , vol.210 , pp. 473-484
    • Heuser, J.1    Griffith, J.2
  • 33
    • 0025186240 scopus 로고
    • Three-stranded paranemic joints: Architecture, topological constraints, and movement
    • Bortner C, Griffith J. Three-stranded paranemic joints: architecture, topological constraints, and movement. J Mol Biol. 215:1990;623-634.
    • (1990) J Mol Biol , vol.215 , pp. 623-634
    • Bortner, C.1    Griffith, J.2
  • 34
    • 0026542543 scopus 로고
    • The apical localization of transcribing RNA polymerases on supercoiled DNA prevents their rotation around the template
    • Heggeler-Bordier BT, Wahli W, Adrian M, Stasiak A, Dubochet J. The apical localization of transcribing RNA polymerases on supercoiled DNA prevents their rotation around the template. EMBO J. 11:1992;667-672.
    • (1992) EMBO J , vol.11 , pp. 667-672
    • Heggeler-Bordier, B.T.1    Wahli, W.2    Adrian, M.3    Stasiak, A.4    Dubochet, J.5
  • 35
    • 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
    • Bednar J, Furrer P, Stasiak A, Dubochet J. The twist, writhe and overall shape of supercoiled DNA change during counterion-induced transition from a loosely to a tightly interwound superhelix. J Mol Biol. 235:1994;825-847.
    • (1994) J Mol Biol , vol.235 , pp. 825-847
    • Bednar, J.1    Furrer, P.2    Stasiak, A.3    Dubochet, J.4
  • 36
    • 0029618936 scopus 로고
    • Determination of DNA persistence length by cryo-electron microscopy. Separation of the static and dynamic contributions to the apparent persistence length of DNA
    • Bednar J, Furrer P, Katritch V, Stasiak A, Dubochet J, Stasiak A. Determination of DNA persistence length by cryo-electron microscopy. Separation of the static and dynamic contributions to the apparent persistence length of DNA. J Mol Biol. 254:1995;579-591.
    • (1995) J Mol Biol , vol.254 , pp. 579-591
    • Bednar, J.1    Furrer, P.2    Katritch, V.3    Stasiak, A.4    Dubochet, J.5    Stasiak, A.6
  • 37
    • 0029866788 scopus 로고    scopus 로고
    • Atomic force microscopy of long and short double-stranded, single-stranded and triple-stranded nucleic acids
    • This work presents a good view of the level of current resolution, and the problems involved in DNA imaging using AFM. of outstanding interest
    • Hansma HG, Revenko I, Kim K, Laney DE. Atomic force microscopy of long and short double-stranded, single-stranded and triple-stranded nucleic acids. Nucleic Acids Res. 24:1996;713-720 This work presents a good view of the level of current resolution, and the problems involved in DNA imaging using AFM. of outstanding interest.
    • (1996) Nucleic Acids Res , vol.24 , pp. 713-720
    • Hansma, H.G.1    Revenko, I.2    Kim, K.3    Laney, D.E.4
  • 38
    • 0028559915 scopus 로고
    • Following the assembly of RNA polymerase - DNA complexes in aqueous solutions with the scanning force microscope
    • Guthold M, Bezanilla M, Erie DA, Jenkins B, Hansma HG, Bustamante C. Following the assembly of RNA polymerase - DNA complexes in aqueous solutions with the scanning force microscope. Proc Natl Acad Sci USA. 91:1994;12927-12931.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12927-12931
    • Guthold, M.1    Bezanilla, M.2    Erie, D.A.3    Jenkins, B.4    Hansma, H.G.5    Bustamante, C.6
  • 39
    • 0028964501 scopus 로고
    • Visualization of nucleosomal substructure in native chromatin by atomic force microscopy
    • Martin LD, Vesenka JP, Henderson E, Dobbs DL. Visualization of nucleosomal substructure in native chromatin by atomic force microscopy. Biochemistry. 34:1995;4610-4616.
    • (1995) Biochemistry , vol.34 , pp. 4610-4616
    • Martin, L.D.1    Vesenka, J.P.2    Henderson, E.3    Dobbs, D.L.4
  • 41
    • 0027984749 scopus 로고
    • Probing chromatin with the scanning force microscope
    • Fritzsche W, Schaper A, Jovin TM. Probing chromatin with the scanning force microscope. Chromosoma. 103:1994;231-236.
    • (1994) Chromosoma , vol.103 , pp. 231-236
    • Fritzsche, W.1    Schaper, A.2    Jovin, T.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.