메뉴 건너뛰기




Volumn 271, Issue 5250, 1996, Pages 778-784

Intercalation, DNA kinking, and the control of transcription

Author keywords

[No Author keywords available]

Indexed keywords

DNA B; INTERCALATING AGENT;

EID: 0030046809     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.271.5250.778     Document Type: Article
Times cited : (263)

References (104)
  • 1
    • 84968731842 scopus 로고
    • R. D. Komberg, Science 184, 868 (1975); A. L. Olins and D E Olins, ibid 183, 330 (1974), K. E. van Holde, B Sahasrabuddhe, R. Shaw, Nucleic Acids Res. 1, 1579 (1974); J. D. Griffith, Science 187, 1202 (1975); J P. Baldwin, P G. Boseley, E M Bradbury, K. Ibel, Nature 253, 245 (1975)
    • (1975) Science , vol.184 , pp. 868
    • Komberg, R.D.1
  • 2
    • 0015964401 scopus 로고
    • R. D. Komberg, Science 184, 868 (1975); A. L. Olins and D E Olins, ibid 183, 330 (1974), K. E. van Holde, B Sahasrabuddhe, R. Shaw, Nucleic Acids Res. 1, 1579 (1974); J. D. Griffith, Science 187, 1202 (1975); J P. Baldwin, P G. Boseley, E M Bradbury, K. Ibel, Nature 253, 245 (1975)
    • (1974) Science , vol.183 , pp. 330
    • Olins, A.L.1    Olins, D.E.2
  • 3
    • 0016133116 scopus 로고
    • R. D. Komberg, Science 184, 868 (1975); A. L. Olins and D E Olins, ibid 183, 330 (1974), K. E. van Holde, B Sahasrabuddhe, R. Shaw, Nucleic Acids Res. 1, 1579 (1974); J. D. Griffith, Science 187, 1202 (1975); J P. Baldwin, P G. Boseley, E M Bradbury, K. Ibel, Nature 253, 245 (1975)
    • (1974) Nucleic Acids Res. , vol.1 , pp. 1579
    • Van Holde, K.E.1    Sahasrabuddhe, B.2    Shaw, R.3
  • 4
    • 0016698606 scopus 로고
    • R. D. Komberg, Science 184, 868 (1975); A. L. Olins and D E Olins, ibid 183, 330 (1974), K. E. van Holde, B Sahasrabuddhe, R. Shaw, Nucleic Acids Res. 1, 1579 (1974); J. D. Griffith, Science 187, 1202 (1975); J P. Baldwin, P G. Boseley, E M Bradbury, K. Ibel, Nature 253, 245 (1975)
    • (1975) Science , vol.187 , pp. 1202
    • Griffith, J.D.1
  • 5
    • 0016634494 scopus 로고
    • R. D. Komberg, Science 184, 868 (1975); A. L. Olins and D E Olins, ibid 183, 330 (1974), K. E. van Holde, B Sahasrabuddhe, R. Shaw, Nucleic Acids Res. 1, 1579 (1974); J. D. Griffith, Science 187, 1202 (1975); J P. Baldwin, P G. Boseley, E M Bradbury, K. Ibel, Nature 253, 245 (1975)
    • (1975) Nature , vol.253 , pp. 245
    • Baldwin, J.P.1    Boseley, P.G.2    Bradbury, E.M.3    Ibel, K.4
  • 7
    • 0023904316 scopus 로고
    • J. C Wang and G. N. Giaever, Science 240, 300 (1988), A. A. Travers, in DNA-Protein: Structural Interactions, D. M. J. Lilley, Ed. (Oxford Univ. Press, New York, 1995), pp 49-75
    • (1988) Science , vol.240 , pp. 300
    • Wang, J.C.1    Giaever, G.N.2
  • 8
    • 0001975345 scopus 로고
    • D. M. J. Lilley, Ed. Oxford Univ. Press, New York
    • J. C Wang and G. N. Giaever, Science 240, 300 (1988), A. A. Travers, in DNA-Protein: Structural Interactions, D. M. J. Lilley, Ed. (Oxford Univ. Press, New York, 1995), pp 49-75
    • (1995) DNA-Protein: Structural Interactions , pp. 49-75
    • Travers, A.A.1
  • 9
    • 0027483012 scopus 로고
    • J. L. Kim, D. B Nikoiov, S K. Burley, Nature 365, 520 (1993); J. L. Kim and S. K Burley, Nature Struct. Biol. 1, 638 (1994), Y Kim, J. H Geiger, S. Hahn, P. B Sigler, Nature 365, 512 (1993).
    • (1993) Nature , vol.365 , pp. 520
    • Kim, J.L.1    Nikoiov, D.B.2    Burley, S.K.3
  • 10
    • 0027974851 scopus 로고
    • J. L. Kim, D. B Nikoiov, S K. Burley, Nature 365, 520 (1993); J. L. Kim and S. K Burley, Nature Struct. Biol. 1, 638 (1994), Y Kim, J. H Geiger, S. Hahn, P. B Sigler, Nature 365, 512 (1993).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 638
    • Kim, J.L.1    Burley, S.K.2
  • 11
    • 0027504913 scopus 로고
    • J. L. Kim, D. B Nikoiov, S K. Burley, Nature 365, 520 (1993); J. L. Kim and S. K Burley, Nature Struct. Biol. 1, 638 (1994), Y Kim, J. H Geiger, S. Hahn, P. B Sigler, Nature 365, 512 (1993).
    • (1993) Nature , vol.365 , pp. 512
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 12
    • 0028785254 scopus 로고
    • M. H. Werner et al , Cell 83, 761 (1995)
    • (1995) Cell , vol.83 , pp. 761
    • Werner, M.H.1
  • 14
    • 0029131298 scopus 로고
    • J. J. Love et al., Nature 376, 791 (1995).
    • (1995) Nature , vol.376 , pp. 791
    • Love, J.J.1
  • 16
    • 0016382119 scopus 로고
    • J. A. Schellman, Biopolymers 13, 217 (1974); F H. C. Crick and A. Klug, Nature 255, 530 (1975); H. M. Sobell, C.-C Tsai, S G Gilbert, S. C. Jain, T. D. Sakore, Proc Natl. Acad Sci. U.S.A. 73, 3068 (1976). With respect to the definitions put forth in this article, kinking of the DNA is distinguished from bending Kinking occurs when 2 bp are unstacked, resulting in an abrupt, local alteration in the direction of the helix axis Bending refers to a more general phenomenon in which a change in the direction of the helix axis can occur with or without unstacking of adjacent base pairs Thus, kinking is one mode of bending, but bending can occur without kinking.
    • (1974) Biopolymers , vol.13 , pp. 217
    • Schellman, J.A.1
  • 17
    • 0016850069 scopus 로고
    • J. A. Schellman, Biopolymers 13, 217 (1974); F H. C. Crick and A. Klug, Nature 255, 530 (1975); H. M. Sobell, C.-C Tsai, S G Gilbert, S. C. Jain, T. D. Sakore, Proc Natl. Acad Sci. U.S.A. 73, 3068 (1976). With respect to the definitions put forth in this article, kinking of the DNA is distinguished from bending Kinking occurs when 2 bp are unstacked, resulting in an abrupt, local alteration in the direction of the helix axis Bending refers to a more general phenomenon in which a change in the direction of the helix axis can occur with or without unstacking of adjacent base pairs Thus, kinking is one mode of bending, but bending can occur without kinking.
    • (1975) Nature , vol.255 , pp. 530
    • Crick, F.H.C.1    Klug, A.2
  • 18
    • 0000127789 scopus 로고
    • With respect to the definitions put forth in this article, kinking of the DNA is distinguished from bending Kinking occurs when 2 bp are unstacked, resulting in an abrupt, local alteration in the direction of the helix axis Bending refers to a more general phenomenon in which a change in the direction of the helix axis can occur with or without unstacking of adjacent base pairs Thus, kinking is one mode of bending, but bending can occur without kinking
    • J. A. Schellman, Biopolymers 13, 217 (1974); F H. C. Crick and A. Klug, Nature 255, 530 (1975); H. M. Sobell, C.-C Tsai, S G Gilbert, S. C. Jain, T. D. Sakore, Proc Natl. Acad Sci. U.S.A. 73, 3068 (1976). With respect to the definitions put forth in this article, kinking of the DNA is distinguished from bending Kinking occurs when 2 bp are unstacked, resulting in an abrupt, local alteration in the direction of the helix axis Bending refers to a more general phenomenon in which a change in the direction of the helix axis can occur with or without unstacking of adjacent base pairs Thus, kinking is one mode of bending, but bending can occur without kinking.
    • (1976) Proc Natl. Acad Sci. U.S.A. , vol.73 , pp. 3068
    • Sobell, H.M.1    Tsai, C.-C.2    Gilbert, S.G.3    Jain, S.C.4    Sakore, T.D.5
  • 19
    • 0027878849 scopus 로고
    • M. S. Searle, Prog. Nucl Magn. Reson Spectrosc. 25, 403 (1993); B. H. Geierstanger and D F. Wemmer, Annu. Rev Biophys. Biomol Struct. 24, 463 (1995).
    • (1993) Prog. Nucl Magn. Reson Spectrosc. , vol.25 , pp. 403
    • Searle, M.S.1
  • 21
    • 13344256387 scopus 로고    scopus 로고
    • note
    • A base step is defined as two consecutive base pairs of DNA Base pairs are formed from four different building blocks as illustrated in Fig 5A. Two of these building blocks hydrogen bond to form a base pair which, when viewed from the minor or major groove edges (Fig. 5B), can be thought of as comprising a single plane. Hence, geometrically, a base pair can be treated as a single plane - a base plane. When one base plane is tilted about its long axis relative to an adjacent base pair, the angle of tilting is defined as roll. Thus, base planes may be "rolled open" relative to each other either toward the minor or major grooves of DNA (Fig 5C). Unwinding of the DNA is accomplished by lowering the degree of twist (Fig. 5C).
  • 22
    • 0018447932 scopus 로고
    • V. B Zhurkin et al., Nucleic Acids Res. 6, 1081 (1979); P. J. Hagerman, Biochem. Biophys. Acta 1131, 125 (1992).
    • (1979) Nucleic Acids Res. , vol.6 , pp. 1081
    • Zhurkin, V.B.1
  • 23
    • 0026642548 scopus 로고
    • V. B Zhurkin et al., Nucleic Acids Res. 6, 1081 (1979); P. J. Hagerman, Biochem. Biophys. Acta 1131, 125 (1992).
    • (1992) Biochem. Biophys. Acta , vol.1131 , pp. 125
    • Hagerman, P.J.1
  • 24
    • 0024373679 scopus 로고
    • A A Travers, Annu. Rev. Biochem 58, 427 (1989), D M Crothers, T. E Haran, J. G. Nadeau, J. Biol. Chem 265, 7093 (1990); T. E. Haran, J. D. Kahn, D. M. Crothers, J. Mol Biol 244, 135 (1994); A. A. Travers, Nature Struct Biol 2, 615 (1995)
    • (1989) Annu. Rev. Biochem , vol.58 , pp. 427
    • Travers, A.A.1
  • 25
    • 0025269492 scopus 로고
    • A A Travers, Annu. Rev. Biochem 58, 427 (1989), D M Crothers, T. E Haran, J. G. Nadeau, J. Biol. Chem 265, 7093 (1990); T. E. Haran, J. D. Kahn, D. M. Crothers, J. Mol Biol 244, 135 (1994); A. A. Travers, Nature Struct Biol 2, 615 (1995)
    • (1990) J. Biol. Chem , vol.265 , pp. 7093
    • Crothers, D.M.1    Haran, T.E.2    Nadeau, J.G.3
  • 26
    • 0028073817 scopus 로고
    • A A Travers, Annu. Rev. Biochem 58, 427 (1989), D M Crothers, T. E Haran, J. G. Nadeau, J. Biol. Chem 265, 7093 (1990); T. E. Haran, J. D. Kahn, D. M. Crothers, J. Mol Biol 244, 135 (1994); A. A. Travers, Nature Struct Biol 2, 615 (1995)
    • (1994) J. Mol Biol , vol.244 , pp. 135
    • Haran, T.E.1    Kahn, J.D.2    Crothers, D.M.3
  • 27
    • 0029103236 scopus 로고
    • A A Travers, Annu. Rev. Biochem 58, 427 (1989), D M Crothers, T. E Haran, J. G. Nadeau, J. Biol. Chem 265, 7093 (1990); T. E. Haran, J. D. Kahn, D. M. Crothers, J. Mol Biol 244, 135 (1994); A. A. Travers, Nature Struct Biol 2, 615 (1995)
    • (1995) Nature Struct Biol , vol.2 , pp. 615
    • Travers, A.A.1
  • 28
    • 0013411169 scopus 로고
    • L. W Keepers, P A. Kollman, P K. Weiner, T. L. James, Proc Natl. Acad. Sci. USA 79, 5537 (1982), M Levitt, Cold Spring Harbor Symp Quant. Biol. 47, 251 (1982); S. J. Weiner, et al., J. Am. Chem Soc 106, 765 (1984); K K Irikura, B. Tidor, B R Brooks, M Karplus, Science 229, 571 (1985), C. Singh, P Weiner, P. A. Kollman, Proc. Natl. Acad. Sci U.S.A 82, 755 (1985); S J. Weiner, P. A Kollman, D. T Nguyen, D. A Case, J. Comp Chem. 7, 230 (1986), S. N. Rao, U. C. Singh, P. A. Kollman, Isr J. Chem. 27, 189 (1986).
    • (1982) Proc Natl. Acad. Sci. USA , vol.79 , pp. 5537
    • Keepers, L.W.1    Kollman, P.A.2    Weiner, P.K.3    James, T.L.4
  • 29
    • 0020262664 scopus 로고
    • L. W Keepers, P A. Kollman, P K. Weiner, T. L. James, Proc Natl. Acad. Sci. USA 79, 5537 (1982), M Levitt, Cold Spring Harbor Symp Quant. Biol. 47, 251 (1982); S. J. Weiner, et al., J. Am. Chem Soc 106, 765 (1984); K K Irikura, B. Tidor, B R Brooks, M Karplus, Science 229, 571 (1985), C. Singh, P Weiner, P. A. Kollman, Proc. Natl. Acad. Sci U.S.A 82, 755 (1985); S J. Weiner, P. A Kollman, D. T Nguyen, D. A Case, J. Comp Chem. 7, 230 (1986), S. N. Rao, U. C. Singh, P. A. Kollman, Isr J. Chem. 27, 189 (1986).
    • (1982) Cold Spring Harbor Symp Quant. Biol. , vol.47 , pp. 251
    • Levitt, M.1
  • 30
    • 0021757436 scopus 로고
    • L. W Keepers, P A. Kollman, P K. Weiner, T. L. James, Proc Natl. Acad. Sci. USA 79, 5537 (1982), M Levitt, Cold Spring Harbor Symp Quant. Biol. 47, 251 (1982); S. J. Weiner, et al., J. Am. Chem Soc 106, 765 (1984); K K Irikura, B. Tidor, B R Brooks, M Karplus, Science 229, 571 (1985), C. Singh, P Weiner, P. A. Kollman, Proc. Natl. Acad. Sci U.S.A 82, 755 (1985); S J. Weiner, P. A Kollman, D. T Nguyen, D. A Case, J. Comp Chem. 7, 230 (1986), S. N. Rao, U. C. Singh, P. A. Kollman, Isr J. Chem. 27, 189 (1986).
    • (1984) J. Am. Chem Soc , vol.106 , pp. 765
    • Weiner, S.J.1
  • 31
    • 0022399917 scopus 로고
    • L. W Keepers, P A. Kollman, P K. Weiner, T. L. James, Proc Natl. Acad. Sci. USA 79, 5537 (1982), M Levitt, Cold Spring Harbor Symp Quant. Biol. 47, 251 (1982); S. J. Weiner, et al., J. Am. Chem Soc 106, 765 (1984); K K Irikura, B. Tidor, B R Brooks, M Karplus, Science 229, 571 (1985), C. Singh, P Weiner, P. A. Kollman, Proc. Natl. Acad. Sci U.S.A 82, 755 (1985); S J. Weiner, P. A Kollman, D. T Nguyen, D. A Case, J. Comp Chem. 7, 230 (1986), S. N. Rao, U. C. Singh, P. A. Kollman, Isr J. Chem. 27, 189 (1986).
    • (1985) Science , vol.229 , pp. 571
    • Irikura, K.K.1    Tidor, B.2    Brooks, B.R.3    Karplus, M.4
  • 32
    • 0007728014 scopus 로고
    • L. W Keepers, P A. Kollman, P K. Weiner, T. L. James, Proc Natl. Acad. Sci. USA 79, 5537 (1982), M Levitt, Cold Spring Harbor Symp Quant. Biol. 47, 251 (1982); S. J. Weiner, et al., J. Am. Chem Soc 106, 765 (1984); K K Irikura, B. Tidor, B R Brooks, M Karplus, Science 229, 571 (1985), C. Singh, P Weiner, P. A. Kollman, Proc. Natl. Acad. Sci U.S.A 82, 755 (1985); S J. Weiner, P. A Kollman, D. T Nguyen, D. A Case, J. Comp Chem. 7, 230 (1986), S. N. Rao, U. C. Singh, P. A. Kollman, Isr J. Chem. 27, 189 (1986).
    • (1985) Proc. Natl. Acad. Sci U.S.A , vol.82 , pp. 755
    • Singh, C.1    Weiner, P.2    Kollman, P.A.3
  • 33
    • 84988053694 scopus 로고
    • L. W Keepers, P A. Kollman, P K. Weiner, T. L. James, Proc Natl. Acad. Sci. USA 79, 5537 (1982), M Levitt, Cold Spring Harbor Symp Quant. Biol. 47, 251 (1982); S. J. Weiner, et al., J. Am. Chem Soc 106, 765 (1984); K K Irikura, B. Tidor, B R Brooks, M Karplus, Science 229, 571 (1985), C. Singh, P Weiner, P. A. Kollman, Proc. Natl. Acad. Sci U.S.A 82, 755 (1985); S J. Weiner, P. A Kollman, D. T Nguyen, D. A Case, J. Comp Chem. 7, 230 (1986), S. N. Rao, U. C. Singh, P. A. Kollman, Isr J. Chem. 27, 189 (1986).
    • (1986) J. Comp Chem. , vol.7 , pp. 230
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 34
    • 85005722912 scopus 로고
    • L. W Keepers, P A. Kollman, P K. Weiner, T. L. James, Proc Natl. Acad. Sci. USA 79, 5537 (1982), M Levitt, Cold Spring Harbor Symp Quant. Biol. 47, 251 (1982); S. J. Weiner, et al., J. Am. Chem Soc 106, 765 (1984); K K Irikura, B. Tidor, B R Brooks, M Karplus, Science 229, 571 (1985), C. Singh, P Weiner, P. A. Kollman, Proc. Natl. Acad. Sci U.S.A 82, 755 (1985); S J. Weiner, P. A Kollman, D. T Nguyen, D. A Case, J. Comp Chem. 7, 230 (1986), S. N. Rao, U. C. Singh, P. A. Kollman, Isr J. Chem. 27, 189 (1986).
    • (1986) Isr J. Chem. , vol.27 , pp. 189
    • Rao, S.N.1    Singh, U.C.2    Kollman, P.A.3
  • 35
    • 0022230224 scopus 로고
    • H R. Drew and A A Travers, J Mol Biol. 186, 773 (1985); S. C Satchwell, H R. Drew, A A. Travers, ibid 191, 659 (1986); C R. Calladine and H. R. Drew, ibid. 192, 907 (1986)
    • (1985) J Mol Biol. , vol.186 , pp. 773
    • Drew, H.R.1    Travers, A.A.2
  • 36
    • 0023001414 scopus 로고
    • H R. Drew and A A Travers, J Mol Biol. 186, 773 (1985); S. C Satchwell, H R. Drew, A A. Travers, ibid 191, 659 (1986); C R. Calladine and H. R. Drew, ibid. 192, 907 (1986)
    • (1986) J Mol Biol. , vol.191 , pp. 659
    • Satchwell, S.C.1    Drew, H.R.2    Travers, A.A.3
  • 37
    • 0022914418 scopus 로고
    • H R. Drew and A A Travers, J Mol Biol. 186, 773 (1985); S. C Satchwell, H R. Drew, A A. Travers, ibid 191, 659 (1986); C R. Calladine and H. R. Drew, ibid. 192, 907 (1986)
    • (1986) J Mol Biol. , vol.192 , pp. 907
    • Calladine, C.R.1    Drew, H.R.2
  • 38
    • 0024300174 scopus 로고
    • M. R Gartenberg and D. M. Crothers, Nature 333, 824 (1988); D. D. Dalma-Weiszhausz, M. R Gartenberg, D. M. Crothers, Nucleic Acids Res 19, 611 (1991)
    • (1988) Nature , vol.333 , pp. 824
    • Gartenberg, M.R.1    Crothers, D.M.2
  • 42
    • 0028289189 scopus 로고
    • M E Hogan, M. W. Roberson, R. H Austin, Proc. Natl. Acad Sci. USA 86, 9273 (1989); J D. Kahn, E. Yun, D. M Crothers, Nature 368, 163 (1994).
    • (1994) Nature , vol.368 , pp. 163
    • Kahn, J.D.1    Yun, E.2    Crothers, D.M.3
  • 44
    • 0028293916 scopus 로고
    • G. B. Koudelka, P. Harbury, S. C. Hamson, M. Ptashne, Proc. Natl Acad. Sci U S A. 85, 4633 (1988); M. Lundin, J. O. Nehlin, H. Ronne, Mol. Cell. Biol 14, 1979 (1994).
    • (1994) Mol. Cell. Biol , vol.14 , pp. 1979
    • Lundin, M.1    Nehlin, J.O.2    Ronne, H.3
  • 46
    • 0021166081 scopus 로고
    • S Cheung, K. Arndt, P. Lu, Proc. Natl. Acad. Sci. U S.A 81, 3665 (1984); D. Battacharyya and M. Bansal, J. Biomol. Struct. Dyn. 8, 539 (1990), K Yanagi, G. G. Prive, R E. Dickerson, J. Mol. Biol. 217, 201 (1991); E. Hassan, thesis, University of Cambridge (1995).
    • (1984) Proc. Natl. Acad. Sci. U S.A , vol.81 , pp. 3665
    • Cheung, S.1    Arndt, K.2    Lu, P.3
  • 47
    • 0025648066 scopus 로고
    • S Cheung, K. Arndt, P. Lu, Proc. Natl. Acad. Sci. U S.A 81, 3665 (1984); D. Battacharyya and M. Bansal, J. Biomol. Struct. Dyn. 8, 539 (1990), K Yanagi, G. G. Prive, R E. Dickerson, J. Mol. Biol. 217, 201 (1991); E. Hassan, thesis, University of Cambridge (1995).
    • (1990) J. Biomol. Struct. Dyn. , vol.8 , pp. 539
    • Battacharyya, D.1    Bansal, M.2
  • 48
    • 0025966606 scopus 로고
    • S Cheung, K. Arndt, P. Lu, Proc. Natl. Acad. Sci. U S.A 81, 3665 (1984); D. Battacharyya and M. Bansal, J. Biomol. Struct. Dyn. 8, 539 (1990), K Yanagi, G. G. Prive, R E. Dickerson, J. Mol. Biol. 217, 201 (1991); E. Hassan, thesis, University of Cambridge (1995).
    • (1991) J. Mol. Biol. , vol.217 , pp. 201
    • Yanagi, K.1    Prive, G.G.2    Dickerson, R.E.3
  • 49
    • 0021166081 scopus 로고
    • thesis, University of Cambridge
    • S Cheung, K. Arndt, P. Lu, Proc. Natl. Acad. Sci. U S.A 81, 3665 (1984); D. Battacharyya and M. Bansal, J. Biomol. Struct. Dyn. 8, 539 (1990), K Yanagi, G. G. Prive, R E. Dickerson, J. Mol. Biol. 217, 201 (1991); E. Hassan, thesis, University of Cambridge (1995).
    • (1995)
    • Hassan, E.1
  • 53
    • 0026643104 scopus 로고
    • K Giese, J. Cox, R. Grosschedl, Cell 69, 185 (1992); V. R. Harley, R. Lovell-Badge, P. N. Goodfellow, Nucleic Acids Res. 22, 1500 (1994).
    • (1992) Cell , vol.69 , pp. 185
    • Giese, K.1    Cox, J.2    Grosschedl, R.3
  • 60
    • 0029080688 scopus 로고    scopus 로고
    • V. Petn, M. Hsieh, M. Brenowitz, Biochemistry 34, 9977 (1995); D. Sun and L. H. Hurley, Chem. Biol. 2, 457 (1995); K. M. Parkhurst, M. Brenowitz, L. J. Parkhurst, personal communication.
    • (1995) Biochemistry , vol.34 , pp. 9977
    • Petn, V.1    Hsieh, M.2    Brenowitz, M.3
  • 61
    • 0029328528 scopus 로고
    • V. Petn, M. Hsieh, M. Brenowitz, Biochemistry 34, 9977 (1995); D. Sun and L. H. Hurley, Chem. Biol. 2, 457 (1995); K. M. Parkhurst, M. Brenowitz, L. J. Parkhurst, personal communication.
    • (1995) Chem. Biol. , vol.2 , pp. 457
    • Sun, D.1    Hurley, L.H.2
  • 62
    • 0029080688 scopus 로고    scopus 로고
    • personal communication
    • V. Petn, M. Hsieh, M. Brenowitz, Biochemistry 34, 9977 (1995); D. Sun and L. H. Hurley, Chem. Biol. 2, 457 (1995); K. M. Parkhurst, M. Brenowitz, L. J. Parkhurst, personal communication.
    • Parkhurst, K.M.1    Brenowitz, M.2    Parkhurst, L.J.3
  • 67
    • 0028580157 scopus 로고
    • A Pontiggia et al , EMBO J 13, 6115 (1994).
    • (1994) EMBO J , vol.13 , pp. 6115
    • Pontiggia, A.1
  • 68
    • 0028010888 scopus 로고
    • S. Klimasauskas, S. Kumar, R. J Roberts, X. Cheng, Cell 76, 357 (1994); X. Cheng, Annu. Rev. Biophys. Biomol. Struct. 24, 293 (1995); X. Cheng, Curr. Opin Struct. Biol. 5, 4 (1995); S Mi, D. Alonso, R. J Roberts, Nucleic Acids Res. 23, 620 (1995).
    • (1994) Cell , vol.76 , pp. 357
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 69
    • 0029163078 scopus 로고
    • S. Klimasauskas, S. Kumar, R. J Roberts, X. Cheng, Cell 76, 357 (1994); X. Cheng, Annu. Rev. Biophys. Biomol. Struct. 24, 293 (1995); X. Cheng, Curr. Opin Struct. Biol. 5, 4 (1995); S Mi, D. Alonso, R. J Roberts, Nucleic Acids Res. 23, 620 (1995).
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 293
    • Cheng, X.1
  • 70
    • 0028946713 scopus 로고
    • S. Klimasauskas, S. Kumar, R. J Roberts, X. Cheng, Cell 76, 357 (1994); X. Cheng, Annu. Rev. Biophys. Biomol. Struct. 24, 293 (1995); X. Cheng, Curr. Opin Struct. Biol. 5, 4 (1995); S Mi, D. Alonso, R. J Roberts, Nucleic Acids Res. 23, 620 (1995).
    • (1995) Curr. Opin Struct. Biol. , vol.5 , pp. 4
    • Cheng, X.1
  • 71
    • 0028937063 scopus 로고
    • S. Klimasauskas, S. Kumar, R. J Roberts, X. Cheng, Cell 76, 357 (1994); X. Cheng, Annu. Rev. Biophys. Biomol. Struct. 24, 293 (1995); X. Cheng, Curr. Opin Struct. Biol. 5, 4 (1995); S Mi, D. Alonso, R. J Roberts, Nucleic Acids Res. 23, 620 (1995).
    • (1995) Nucleic Acids Res. , vol.23 , pp. 620
    • Mi, S.1    Alonso, D.2    Roberts, R.J.3
  • 73
    • 0024340762 scopus 로고    scopus 로고
    • L. Moitoso de Vargas, S. Kim, A Landy, Science 244, 1457 (1989); H. A. Nash, Trends Biochem Sci 15, 222 (1990), H. A. Nash, in Regulation of Gene Expression in Escherichia coli, E. C. C. Un and A. S. Lynch, Eds., in press. Cis-acting element refers to a protein whose actions are felt at the same DNA locus at which it binds.
    • (1989) Science , vol.244 , pp. 1457
    • Moitoso De Vargas, L.1    Kim, S.2    Landy, A.3
  • 74
    • 0025285536 scopus 로고
    • L. Moitoso de Vargas, S. Kim, A Landy, Science 244, 1457 (1989); H. A. Nash, Trends Biochem Sci 15, 222 (1990), H. A. Nash, in Regulation of Gene Expression in Escherichia coli, E. C. C. Un and A. S. Lynch, Eds., in press. Cis-acting element refers to a protein whose actions are felt at the same DNA locus at which it binds.
    • (1990) Trends Biochem Sci , vol.15 , pp. 222
    • Nash, H.A.1
  • 75
    • 0024340762 scopus 로고    scopus 로고
    • E. C. C. Un and A. S. Lynch, Eds., in press. Cis-acting element refers to a protein whose actions are felt at the same DNA locus at which it binds
    • L. Moitoso de Vargas, S. Kim, A Landy, Science 244, 1457 (1989); H. A. Nash, Trends Biochem Sci 15, 222 (1990), H. A. Nash, in Regulation of Gene Expression in Escherichia coli, E. C. C. Un and A. S. Lynch, Eds., in press. Cis-acting element refers to a protein whose actions are felt at the same DNA locus at which it binds.
    • Regulation of Gene Expression in Escherichia Coli
    • Nash, H.A.1
  • 76
    • 0024424261 scopus 로고
    • S D. Goodman and H. A Nash, Nature 341, 251 (1989); A. M. Segall, S. D. Goodman, H. A. Nash, EMBO J. 13, 4536 (1994).
    • (1989) Nature , vol.341 , pp. 251
    • Goodman, S.D.1    Nash, H.A.2
  • 79
    • 0023500809 scopus 로고
    • E. Giniger and M. Ptashne, Nature 330, 670 (1987); P. B. Sigler, ibid. 333, 210 (1988); L Donaldson and J. P Capone, J. Biol. Chem. 267, 1411 (1992); P. O'Hare and G. Williams, Biochemistry 31, 4150 (1992).
    • (1987) Nature , vol.330 , pp. 670
    • Giniger, E.1    Ptashne, M.2
  • 80
    • 0024291679 scopus 로고
    • E. Giniger and M. Ptashne, Nature 330, 670 (1987); P. B. Sigler, ibid. 333, 210 (1988); L Donaldson and J. P Capone, J. Biol. Chem. 267, 1411 (1992); P. O'Hare and G. Williams, Biochemistry 31, 4150 (1992).
    • (1988) Nature , vol.333 , pp. 210
    • Sigler, P.B.1
  • 81
    • 0026540830 scopus 로고
    • E. Giniger and M. Ptashne, Nature 330, 670 (1987); P. B. Sigler, ibid. 333, 210 (1988); L Donaldson and J. P Capone, J. Biol. Chem. 267, 1411 (1992); P. O'Hare and G. Williams, Biochemistry 31, 4150 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 1411
    • Donaldson, L.1    Capone, J.P.2
  • 82
    • 0026704229 scopus 로고
    • E. Giniger and M. Ptashne, Nature 330, 670 (1987); P. B. Sigler, ibid. 333, 210 (1988); L Donaldson and J. P Capone, J. Biol. Chem. 267, 1411 (1992); P. O'Hare and G. Williams, Biochemistry 31, 4150 (1992).
    • (1992) Biochemistry , vol.31 , pp. 4150
    • O'Hare, P.1    Williams, G.2
  • 84
  • 85
    • 0028978670 scopus 로고
    • D. B. Nikolov et al., Nature 377, 119 (1995).
    • (1995) Nature , vol.377 , pp. 119
    • Nikolov, D.B.1
  • 86
  • 88
    • 13344273832 scopus 로고
    • Bending without intercalation or exclusive minor groove binding occurs in the protein-DNA complexes of several transcription factors from prokaryotes and eukaryotes, for example, E coli CAP protein [S. C. Schulte, G. C. Shields, T. A. Steitz, Science 253, 101 (1991)], HNF3/forkhead [K. L. Clark, E. D. Halay, E Lai, S K Burley, Nature 364, 412 (1993)], and the a1/α2 homeodomain [T. Li, M. R. Stark, A. D. Johnson, C. Wolberger, Science 270, 262 (1995)]. Kinking occurs in several DNA enzymes without intercalation, for example, deoxyribonuclease 1 [S. A Weston, A. Lahm, D. Suck, J. Mol Biol. 226, 1237 (1992)], Eco RV [F. K. Winkler et al., EMBO J 12, 1781 (1993)], and Eco RI [J A. McClarin et al., Science 234, 1526 (1986)]
    • (1991) Science , vol.253 , pp. 101
    • Schulte, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 89
    • 0027270989 scopus 로고
    • Bending without intercalation or exclusive minor groove binding occurs in the protein-DNA complexes of several transcription factors from prokaryotes and eukaryotes, for example, E coli CAP protein [S. C. Schulte, G. C. Shields, T. A. Steitz, Science 253, 101 (1991)], HNF3/forkhead [K. L. Clark, E. D. Halay, E Lai, S K Burley, Nature 364, 412 (1993)], and the a1/α2 homeodomain [T. Li, M. R. Stark, A. D. Johnson, C. Wolberger, Science 270, 262 (1995)]. Kinking occurs in several DNA enzymes without intercalation, for example, deoxyribonuclease 1 [S. A Weston, A. Lahm, D. Suck, J. Mol Biol. 226, 1237 (1992)], Eco RV [F. K. Winkler et al., EMBO J 12, 1781 (1993)], and Eco RI [J A. McClarin et al., Science 234, 1526 (1986)]
    • (1993) Nature , vol.364 , pp. 412
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 90
    • 0028828745 scopus 로고
    • Bending without intercalation or exclusive minor groove binding occurs in the protein-DNA complexes of several transcription factors from prokaryotes and eukaryotes, for example, E coli CAP protein [S. C. Schulte, G. C. Shields, T. A. Steitz, Science 253, 101 (1991)], HNF3/forkhead [K. L. Clark, E. D. Halay, E Lai, S K Burley, Nature 364, 412 (1993)], and the a1/α2 homeodomain [T. Li, M. R. Stark, A. D. Johnson, C. Wolberger, Science 270, 262 (1995)]. Kinking occurs in several DNA enzymes without intercalation, for example, deoxyribonuclease 1 [S. A Weston, A. Lahm, D. Suck, J. Mol Biol. 226, 1237 (1992)], Eco RV [F. K. Winkler et al., EMBO J 12, 1781 (1993)], and Eco RI [J A. McClarin et al., Science 234, 1526 (1986)]
    • (1995) Science , vol.270 , pp. 262
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 91
    • 0026447731 scopus 로고
    • Bending without intercalation or exclusive minor groove binding occurs in the protein-DNA complexes of several transcription factors from prokaryotes and eukaryotes, for example, E coli CAP protein [S. C. Schulte, G. C. Shields, T. A. Steitz, Science 253, 101 (1991)], HNF3/forkhead [K. L. Clark, E. D. Halay, E Lai, S K Burley, Nature 364, 412 (1993)], and the a1/α2 homeodomain [T. Li, M. R. Stark, A. D. Johnson, C. Wolberger, Science 270, 262 (1995)]. Kinking occurs in several DNA enzymes without intercalation, for example, deoxyribonuclease 1 [S. A Weston, A. Lahm, D. Suck, J. Mol Biol. 226, 1237 (1992)], Eco RV [F. K. Winkler et al., EMBO J 12, 1781 (1993)], and Eco RI [J A. McClarin et al., Science 234, 1526 (1986)]
    • (1992) J. Mol Biol. , vol.226 , pp. 1237
    • Weston, S.A.1    Lahm, A.2    Suck, D.3
  • 92
    • 0027159254 scopus 로고
    • Bending without intercalation or exclusive minor groove binding occurs in the protein-DNA complexes of several transcription factors from prokaryotes and eukaryotes, for example, E coli CAP protein [S. C. Schulte, G. C. Shields, T. A. Steitz, Science 253, 101 (1991)], HNF3/forkhead [K. L. Clark, E. D. Halay, E Lai, S K Burley, Nature 364, 412 (1993)], and the a1/α2 homeodomain [T. Li, M. R. Stark, A. D. Johnson, C. Wolberger, Science 270, 262 (1995)]. Kinking occurs in several DNA enzymes without intercalation, for example, deoxyribonuclease 1 [S. A Weston, A. Lahm, D. Suck, J. Mol Biol. 226, 1237 (1992)], Eco RV [F. K. Winkler et al., EMBO J 12, 1781 (1993)], and Eco RI [J A. McClarin et al., Science 234, 1526 (1986)]
    • (1993) EMBO J , vol.12 , pp. 1781
    • Winkler, F.K.1
  • 93
    • 0022964809 scopus 로고
    • Bending without intercalation or exclusive minor groove binding occurs in the protein-DNA complexes of several transcription factors from prokaryotes and eukaryotes, for example, E coli CAP protein [S. C. Schulte, G. C. Shields, T. A. Steitz, Science 253, 101 (1991)], HNF3/forkhead [K. L. Clark, E. D. Halay, E Lai, S K Burley, Nature 364, 412 (1993)], and the a1/α2 homeodomain [T. Li, M. R. Stark, A. D. Johnson, C. Wolberger, Science 270, 262 (1995)]. Kinking occurs in several DNA enzymes without intercalation, for example, deoxyribonuclease 1 [S. A Weston, A. Lahm, D. Suck, J. Mol Biol. 226, 1237 (1992)], Eco RV [F. K. Winkler et al., EMBO J 12, 1781 (1993)], and Eco RI [J A. McClarin et al., Science 234, 1526 (1986)]
    • (1986) Science , vol.234 , pp. 1526
    • McClarin, J.A.1
  • 95
    • 0026742978 scopus 로고
    • H. M. Berman et al., Biophys J 63, 751 (1992); A. A. Gorin, V Zhurkin, W. K Olson, J Biomol Struct. Dyn. 12, a074 (1995)
    • (1992) Biophys J , vol.63 , pp. 751
    • Berman, H.M.1
  • 97
    • 13344264045 scopus 로고    scopus 로고
    • note
    • The coordinates for the LEF-1-DNA complex of Love et al. (7) were not made available to us at the time of writing The structure ot both the protein and the DNA, however, are nearly identical to the structured the SRY-DNA complex (6) at the site of intercalation.
  • 99
    • 0028184697 scopus 로고
    • N Boutonnet, X Hui, K. Zakrzewska, Biopolymers 33, 479 (1993); E Stofer and R. Lavery, ibid 34, 337 (1994).
    • (1994) Biopolymers , vol.34 , pp. 337
    • Stofer, E.1    Lavery, R.2
  • 101
    • 0000449348 scopus 로고
    • M. Carson, J. Appl Crystallogr 24, 958 (1991); J. Mol. Graphics 5, 103 (1987).
    • (1987) J. Mol. Graphics , vol.5 , pp. 103
  • 104
    • 13344254632 scopus 로고    scopus 로고
    • note
    • We wish to acknowledge W. A. Eaton, A. Szabo, H A Nash, and V. Zhurkin for critical reading of the manuscript; J. Aarons for help with the art work in Fig. 3; V. Zhurkin for assistance with the analysis of distorted DNA structures and many stimulating discussions, A. A. Gonn, V. Zhurkin, and W. K. Olson for the use of CompDNA; R. G. Brennan, W. I. Lipscomb, S. K. Burley, and X. Cheng for providing crystal structure coordinates; and M. Summers, R J. Fisher, M. Brenowitz, P. Rice, S.-W. Yang, K. Mizuuchi, and H. A Nash for communicating information before publication Supported by the AIDS Targeted Antiviral Program of the Office of the Director of the National Institutes of Health (G.M.C and A.M.G.)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.