메뉴 건너뛰기




Volumn 46, Issue 44, 2007, Pages 12530-12542

Saccharomyces cerevisiae Hop1 protein zinc finger motif binds to the holliday junction and distorts the DNA structure: Implications for holliday junction migration

Author keywords

[No Author keywords available]

Indexed keywords

MEIOSIS; MUTANT ALLELE; ZINC FINGER MOTIF (ZNF);

EID: 35848931247     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701078v     Document Type: Article
Times cited : (5)

References (60)
  • 1
    • 0029032723 scopus 로고
    • Zinc Fingers
    • Klug, A., and Schwabe, J. W. (1995) Zinc Fingers, FASEB J. 9, 597-604.
    • (1995) FASEB J , vol.9 , pp. 597-604
    • Klug, A.1    Schwabe, J.W.2
  • 2
    • 0034923498 scopus 로고    scopus 로고
    • Design and selection of novel Cys2His2 zinc finger proteins
    • Pabo, C. O., Peisach, E., and Grant, R. A. (2001) Design and selection of novel Cys2His2 zinc finger proteins, Annu. Rev. Biochem. 70, 313-340.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 313-340
    • Pabo, C.O.1    Peisach, E.2    Grant, R.A.3
  • 4
    • 33344464022 scopus 로고    scopus 로고
    • Designer zinc finger proteins: Tools for creating artificial DNA-binding functional proteins
    • Dhanasekaran, M., Negi, S., and Sugiura, Y (2006) Designer zinc finger proteins: Tools for creating artificial DNA-binding functional proteins, Acc. Chem. Res. 39, 45-52.
    • (2006) Acc. Chem. Res , vol.39 , pp. 45-52
    • Dhanasekaran, M.1    Negi, S.2    Sugiura, Y.3
  • 6
    • 0032509320 scopus 로고    scopus 로고
    • Zinc fingers in Caenorhabditis elegans: Finding families and probing pathways
    • Clarke, N. D., and Berg, J. M. (1998) Zinc fingers in Caenorhabditis elegans: finding families and probing pathways, Science 282, 2018-2022.
    • (1998) Science , vol.282 , pp. 2018-2022
    • Clarke, N.D.1    Berg, J.M.2
  • 7
    • 0026071771 scopus 로고
    • Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains
    • Vallee, B. L., Coleman, J. E., and Auld, D. S. (1991) Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains, Proc. Natl. Acad. Sci. U.S.A. 88, 999-1003.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 999-1003
    • Vallee, B.L.1    Coleman, J.E.2    Auld, D.S.3
  • 8
    • 33749236250 scopus 로고    scopus 로고
    • A fungal family of transcriptional regulators: The zinc cluster proteins
    • MacPherson, S., Larochelle, M., and Turcotte, B. (2006) A fungal family of transcriptional regulators: the zinc cluster proteins, Microbiol. Mol. Biol. Rev. 70, 583-604.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 583-604
    • MacPherson, S.1    Larochelle, M.2    Turcotte, B.3
  • 9
    • 0029664453 scopus 로고    scopus 로고
    • The single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high affinity specific DNA binding
    • Pedone, P. V., Ghirlando, R., Clore, G. M., Gronenborn, A. M., Felsenfeld, G., and Omichinski, J. G. (1996) The single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high affinity specific DNA binding, Proc. Natl. Acad. Sci. U.S.A. 93, 2822-2826.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 2822-2826
    • Pedone, P.V.1    Ghirlando, R.2    Clore, G.M.3    Gronenborn, A.M.4    Felsenfeld, G.5    Omichinski, J.G.6
  • 11
    • 0024635860 scopus 로고
    • HOP1: A yeast meiotic pairing gene
    • Hollingsworth, N. M., and Byers, B. (1989) HOP1: a yeast meiotic pairing gene, Genetics 121, 445-462.
    • (1989) Genetics , vol.121 , pp. 445-462
    • Hollingsworth, N.M.1    Byers, B.2
  • 12
    • 0033816350 scopus 로고    scopus 로고
    • Woltering, D., Baumgartner, B., Bagchi, S., Larkin, B., Loidl, J., de los Santos, T., and Hollingsworth, N. M. (2000) Meiotic segregation, synapsis, and recombination checkpoint functions require physical interaction between the chromosomal proteins Red1p and Hop1p, Mol. Cell. Biol. 20, 6646-6658.
    • Woltering, D., Baumgartner, B., Bagchi, S., Larkin, B., Loidl, J., de los Santos, T., and Hollingsworth, N. M. (2000) Meiotic segregation, synapsis, and recombination checkpoint functions require physical interaction between the chromosomal proteins Red1p and Hop1p, Mol. Cell. Biol. 20, 6646-6658.
  • 13
    • 0028178793 scopus 로고
    • Identification of joint molecules that form frequently between homologs but rarely between sister chromatids during yeast meiosis
    • Schwacha, A., and Kleckner, N. (1994) Identification of joint molecules that form frequently between homologs but rarely between sister chromatids during yeast meiosis, Cell 76, 51-63.
    • (1994) Cell , vol.76 , pp. 51-63
    • Schwacha, A.1    Kleckner, N.2
  • 14
    • 0029743465 scopus 로고    scopus 로고
    • Analysis of meiotic recombination pathways in the yeast Saccharomyces cerevisiae
    • Mao-Draayer, Y., Galbraith, A. M., Pittman, D. L., Cool, M., and Malone, R. E. (1996) Analysis of meiotic recombination pathways in the yeast Saccharomyces cerevisiae, Genetics 144, 71-86.
    • (1996) Genetics , vol.144 , pp. 71-86
    • Mao-Draayer, Y.1    Galbraith, A.M.2    Pittman, D.L.3    Cool, M.4    Malone, R.E.5
  • 15
    • 23944442791 scopus 로고    scopus 로고
    • Molecular aspects of meiotic chromosome synapsis and recombination
    • Anuradha, S., and Muniyappa, K. (2005) Molecular aspects of meiotic chromosome synapsis and recombination, Prog. Nucleic Acids Res. Mol. Biol. 79, 49-132.
    • (2005) Prog. Nucleic Acids Res. Mol. Biol , vol.79 , pp. 49-132
    • Anuradha, S.1    Muniyappa, K.2
  • 16
    • 0025259128 scopus 로고
    • The HOP1 gene encodes a meiosis-specific component of yeast chromosomes
    • Hollingsworth, N. M., Goetsch, L., and Byers, B. (1990) The HOP1 gene encodes a meiosis-specific component of yeast chromosomes, Cell 61, 73-84.
    • (1990) Cell , vol.61 , pp. 73-84
    • Hollingsworth, N.M.1    Goetsch, L.2    Byers, B.3
  • 17
    • 13944259727 scopus 로고    scopus 로고
    • Finding and keeping your partner during meiosis
    • Couteau, F., Goodyear, W., and Zetka, M. (2004) Finding and keeping your partner during meiosis, Cell Cycle 3, 1014-1016.
    • (2004) Cell Cycle , vol.3 , pp. 1014-1016
    • Couteau, F.1    Goodyear, W.2    Zetka, M.3
  • 18
    • 0030899885 scopus 로고    scopus 로고
    • The yeast Red1 protein localizes to the cores of meiotic chromosomes
    • Smith, A. V., and Roeder, G. S. (1997). The yeast Red1 protein localizes to the cores of meiotic chromosomes, J. Cell Biol. 136, 957-967.
    • (1997) J. Cell Biol , vol.136 , pp. 957-967
    • Smith, A.V.1    Roeder, G.S.2
  • 19
    • 0030930119 scopus 로고    scopus 로고
    • Genetic interactions between HOP1, RED1 and MEK1 suggest that MEK1 regulates assembly of axial element components during meiosis in the yeast Saccharomyces cerevisiae
    • Hollingsworth, N. M., and Ponte, L. (1997). Genetic interactions between HOP1, RED1 and MEK1 suggest that MEK1 regulates assembly of axial element components during meiosis in the yeast Saccharomyces cerevisiae, Genetics 147, 33-42.
    • (1997) Genetics , vol.147 , pp. 33-42
    • Hollingsworth, N.M.1    Ponte, L.2
  • 20
    • 2642703473 scopus 로고    scopus 로고
    • DNA-binding activities of Hop1 protein, a synaptonemal complex component from Saccharomyces cerevisiae
    • Kironmai, K. M., Muniyappa, K., Friedman, D. B., Hollingsworth, N. M., and Byers, B. (1998) DNA-binding activities of Hop1 protein, a synaptonemal complex component from Saccharomyces cerevisiae, Mol. Cell. Biol. 18, 1424-1435.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1424-1435
    • Kironmai, K.M.1    Muniyappa, K.2    Friedman, D.B.3    Hollingsworth, N.M.4    Byers, B.5
  • 21
    • 0028055220 scopus 로고
    • Insertional mutations in the yeast HOP1 gene: Evidence for multimeric assembly in meiosis
    • Freidman, D. B., Hollingsworth, N. M., and Byers, B. (1994) Insertional mutations in the yeast HOP1 gene: evidence for multimeric assembly in meiosis, Genetics 136, 449-464.
    • (1994) Genetics , vol.136 , pp. 449-464
    • Freidman, D.B.1    Hollingsworth, N.M.2    Byers, B.3
  • 22
    • 33750934915 scopus 로고    scopus 로고
    • Selective Binding of Meiosis-specific Yeast Hop1 Protein to the Holliday Junctions Distorts the DNA Structure and Its Implications for Junction Migration and Resolution
    • Tripathi, P., Anuradha, S., Ghosal, G., and Muniyappa, K. (2006) Selective Binding of Meiosis-specific Yeast Hop1 Protein to the Holliday Junctions Distorts the DNA Structure and Its Implications for Junction Migration and Resolution, J. Mol. Biol. 364, 599-611.
    • (2006) J. Mol. Biol , vol.364 , pp. 599-611
    • Tripathi, P.1    Anuradha, S.2    Ghosal, G.3    Muniyappa, K.4
  • 24
    • 0025248057 scopus 로고
    • The three-way DNA junction is a Y-shaped molecule in which there is no helix-helix stacking
    • Duckett, D. R., and Lilley, D. M. (1990) The three-way DNA junction is a Y-shaped molecule in which there is no helix-helix stacking, EMBO J. 9, 1659-1664.
    • (1990) EMBO J , vol.9 , pp. 1659-1664
    • Duckett, D.R.1    Lilley, D.M.2
  • 27
    • 0028219162 scopus 로고
    • A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in Polyacrylamide gels
    • Nesterenko, M. V., Tilley, J., and Upton, S. J. (1994) A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in Polyacrylamide gels, J. Biochem. Biophys. Methods 28, 239-242.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 239-242
    • Nesterenko, M.V.1    Tilley, J.2    Upton, S.J.3
  • 28
    • 0018846636 scopus 로고
    • Sequencing end-labeled DNA with base-specific chemical cleavages
    • Maxam, A. M., and Gilbert, W. (1980) Sequencing end-labeled DNA with base-specific chemical cleavages, Methods Enzymol. 65, 499-560.
    • (1980) Methods Enzymol , vol.65 , pp. 499-560
    • Maxam, A.M.1    Gilbert, W.2
  • 29
    • 0038634975 scopus 로고    scopus 로고
    • Improvement of the GenTHREADER method for genomic fold recognition
    • McGuffin, L. J., and Jones, D. T. (2003) Improvement of the GenTHREADER method for genomic fold recognition, Bioinformatics 19, 874-881.
    • (2003) Bioinformatics , vol.19 , pp. 874-881
    • McGuffin, L.J.1    Jones, D.T.2
  • 30
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced Genome Annotation using Structural Profiles in the Program 3D-PSSM
    • Kelley, L. A., MacCallum, R. M., and Sternberg, M. J. E. (2000) Enhanced Genome Annotation using Structural Profiles in the Program 3D-PSSM, J. Mol. Biol. 299, 499-520.
    • (2000) J. Mol. Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 31
    • 0037058927 scopus 로고    scopus 로고
    • The directional atomic solvation energy: An atom-based potential for the assignment of protein sequences to known folds
    • Mallick, P., Weiss, R., and Eisenberg, D. (2002) The directional atomic solvation energy: an atom-based potential for the assignment of protein sequences to known folds, Proc. Natl. Acad. Sci. U.S.A. 99, 16041-16046.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 16041-16046
    • Mallick, P.1    Weiss, R.2    Eisenberg, D.3
  • 32
    • 0024571640 scopus 로고
    • The helix-turn-helix DNA binding motif
    • Brennan, R. G., and Matthews, B. W. (1989) The helix-turn-helix DNA binding motif, J. Biol. Chem. 264, 1903-1906.
    • (1989) J. Biol. Chem , vol.264 , pp. 1903-1906
    • Brennan, R.G.1    Matthews, B.W.2
  • 33
    • 3142729487 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Hop1 zinc finger motif is the minimal region required for its function in vitro
    • Anuradha, S., and Muniyappa, K. (2004) Saccharomyces cerevisiae Hop1 zinc finger motif is the minimal region required for its function in vitro, J. Biol. Chem. 279, 28961-28969.
    • (2004) J. Biol. Chem , vol.279 , pp. 28961-28969
    • Anuradha, S.1    Muniyappa, K.2
  • 34
    • 0032562544 scopus 로고    scopus 로고
    • Structural recognition and distortion by the DNA junction-resolving enzyme RusA
    • Giraud-Panis, M.-J. E., and Lilley, D. M. J. (1998) Structural recognition and distortion by the DNA junction-resolving enzyme RusA, J. Mol. Biol. 278, 117-133.
    • (1998) J. Mol. Biol , vol.278 , pp. 117-133
    • Giraud-Panis, M.-J.E.1    Lilley, D.M.J.2
  • 35
    • 18744364456 scopus 로고    scopus 로고
    • Holliday junction-binding peptides inhibit distinct junction-processing enzymes
    • Kepple, K. V., Boldt, J. L., and Segall, A. M. (2005) Holliday junction-binding peptides inhibit distinct junction-processing enzymes, Proc. Natl. Acad. Sci. U.S.A. 102, 6867-6872.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 6867-6872
    • Kepple, K.V.1    Boldt, J.L.2    Segall, A.M.3
  • 36
    • 14844293868 scopus 로고    scopus 로고
    • Peptide trapping of the Holliday junction intermediate in Cre-1oxP site-specific recombination
    • Ghosh, K., Lau, C. K., Guao, F., Segall, A. M., and Van Duyne, G. D. (2005) Peptide trapping of the Holliday junction intermediate in Cre-1oxP site-specific recombination, J. Biol. Chem. 280, 8290-8299.
    • (2005) J. Biol. Chem , vol.280 , pp. 8290-8299
    • Ghosh, K.1    Lau, C.K.2    Guao, F.3    Segall, A.M.4    Van Duyne, G.D.5
  • 37
    • 33749987030 scopus 로고    scopus 로고
    • New peptide inhibitors of type IB topoisomerases: Similarities and differences vis-a-vis inhibitors of tyrosine recombinases
    • Fujimoto, D. F., Pinilla, C., and Segall, A. M. (2006) New peptide inhibitors of type IB topoisomerases: similarities and differences vis-a-vis inhibitors of tyrosine recombinases, J. Mol. Biol. 363, 891-907.
    • (2006) J. Mol. Biol , vol.363 , pp. 891-907
    • Fujimoto, D.F.1    Pinilla, C.2    Segall, A.M.3
  • 38
    • 0026346185 scopus 로고
    • Gel retardation
    • Carey, J. (1991) Gel retardation, Methods Enzymol. 208, 103-117.
    • (1991) Methods Enzymol , vol.208 , pp. 103-117
    • Carey, J.1
  • 39
    • 0035366324 scopus 로고    scopus 로고
    • The crystal structures of DNA Holliday junctions
    • Ho, P. S., and Eichman, B. F. (2001) The crystal structures of DNA Holliday junctions, Curr. Opin. Struct. Biol. 11, 302-308.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 302-308
    • Ho, P.S.1    Eichman, B.F.2
  • 41
    • 0037313186 scopus 로고    scopus 로고
    • Watching flipping junctions
    • Churchill, M. E. A. (2003) Watching flipping junctions, Nat. Struct. Biol. 10, 73-75.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 73-75
    • Churchill, M.E.A.1
  • 42
    • 0014977511 scopus 로고
    • The permanganate oxidation of thymidine and thymidylic acid
    • Iida, S., and Hayatsu, H. (1971) The permanganate oxidation of thymidine and thymidylic acid, Biochim. Biophys. Acta 228, 1-8.
    • (1971) Biochim. Biophys. Acta , vol.228 , pp. 1-8
    • Iida, S.1    Hayatsu, H.2
  • 43
    • 0034681277 scopus 로고    scopus 로고
    • Extensive central disruption of a four-way junction on binding CCE1 resolving enzyme
    • DeClais, A.-C., and Lilley, D. M. J. (2000) Extensive central disruption of a four-way junction on binding CCE1 resolving enzyme, J. Mol. Biol. 296, 421-433.
    • (2000) J. Mol. Biol , vol.296 , pp. 421-433
    • DeClais, A.-C.1    Lilley, D.M.J.2
  • 44
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • West, S. C. (2003). Molecular views of recombination proteins and their control, Nat. Rev. Mol. Cell Biol. 4, 435-445.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 435-445
    • West, S.C.1
  • 45
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity, J. H., Lee, B. M., and Wright, P. E. (2001) Zinc finger proteins: new insights into structural and functional diversity, Curr. Opin. Struct. Biol. 11, 39-46.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 39-46
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 46
    • 0030595337 scopus 로고    scopus 로고
    • Structural classification of HTH DNA-binding domains and protein-DNA interaction modes
    • Wintjens, R., and Rooman, M. (1996) Structural classification of HTH DNA-binding domains and protein-DNA interaction modes, J. Mol. Biol. 262, 294-313.
    • (1996) J. Mol. Biol , vol.262 , pp. 294-313
    • Wintjens, R.1    Rooman, M.2
  • 48
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma complex of E. coli DNA polymerase III
    • Jeruzalmi, D., O'Donnell, M., and Kuriyan, J. (2001) Crystal structure of the processivity clamp loader gamma complex of E. coli DNA polymerase III, Cell 106, 429-441.
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 49
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton, M. R., Scaife, S., and Wigley, D. B. (2001) Structural analysis of DNA replication fork reversal by RecG, Cell 107, 79-89.
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 50
    • 17144385089 scopus 로고    scopus 로고
    • DNA binding by the substrate specificity (wedge) domain of RecG helicase suggests a role in processivity
    • Briggs, G. S., Mahdi, A. A., Wen, Q., and Lloyd, R. G. (2005) DNA binding by the substrate specificity (wedge) domain of RecG helicase suggests a role in processivity, J. Biol. Chem. 280, 13921-13927.
    • (2005) J. Biol. Chem , vol.280 , pp. 13921-13927
    • Briggs, G.S.1    Mahdi, A.A.2    Wen, Q.3    Lloyd, R.G.4
  • 51
    • 0030885346 scopus 로고    scopus 로고
    • DNA binding and helicase domains of the Escherichia coli recombination protein RecG
    • Mahdi, A. A., McGlynn, P., Levett, S. D., and Lloyd, R. G. (1997) DNA binding and helicase domains of the Escherichia coli recombination protein RecG, Nucleic Acids Res. 25, 3875-3880.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3875-3880
    • Mahdi, A.A.1    McGlynn, P.2    Levett, S.D.3    Lloyd, R.G.4
  • 52
    • 0033588108 scopus 로고    scopus 로고
    • Flexible zinc finger requirement for binding of the transcriptional activator staf to U6 small nuclear RNA and tRNA(Sec) promoters
    • Schaub, M., Krol, A., and Carbon, P. (1999) Flexible zinc finger requirement for binding of the transcriptional activator staf to U6 small nuclear RNA and tRNA(Sec) promoters, J. Biol. Chem. 274, 24241-24249.
    • (1999) J. Biol. Chem , vol.274 , pp. 24241-24249
    • Schaub, M.1    Krol, A.2    Carbon, P.3
  • 53
    • 0031820966 scopus 로고    scopus 로고
    • Specific RNA binding proteins constructed from zinc fingers
    • Friesen, W. J., and Darby, M. K. (1998) Specific RNA binding proteins constructed from zinc fingers, Nat. Struct. Biol. 5, 543-546.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 543-546
    • Friesen, W.J.1    Darby, M.K.2
  • 54
    • 0033578395 scopus 로고    scopus 로고
    • Dimerization of zinc fingers mediated by peptides evolved in vitro from random sequences
    • Wang, B. S., and Pabo, C. O. (1999) Dimerization of zinc fingers mediated by peptides evolved in vitro from random sequences, Proc. Natl. Acad. Sci. U.S.A. 96, 9568-9573.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 9568-9573
    • Wang, B.S.1    Pabo, C.O.2
  • 55
    • 0031011235 scopus 로고    scopus 로고
    • The N-terminal fingers of chicken GATA-2 and GATA-3 are independent sequence-specific DNA binding domains
    • Pedone, P. V., Omichinski, J. G., Nony, P., Trainor, C., Gronenborn, A. M., Clore, G. M., and Felsenfeld, G. (1997) The N-terminal fingers of chicken GATA-2 and GATA-3 are independent sequence-specific DNA binding domains, EMBO J. 16, 2874-2882.
    • (1997) EMBO J , vol.16 , pp. 2874-2882
    • Pedone, P.V.1    Omichinski, J.G.2    Nony, P.3    Trainor, C.4    Gronenborn, A.M.5    Clore, G.M.6    Felsenfeld, G.7
  • 56
    • 0031013382 scopus 로고    scopus 로고
    • The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode
    • Omichinski, J. G., Pedone, P. V., Felsenfeld, G., Gronenborn, A. M., and Clore, G. M. (1997) The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode, Nat. Struct. Biol. 4, 122-130.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 122-130
    • Omichinski, J.G.1    Pedone, P.V.2    Felsenfeld, G.3    Gronenborn, A.M.4    Clore, G.M.5
  • 57
    • 0242581682 scopus 로고    scopus 로고
    • Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition
    • Lu, D., Searles, M. A., and Klug, A. (2003) Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition, Nature 426, 96-100.
    • (2003) Nature , vol.426 , pp. 96-100
    • Lu, D.1    Searles, M.A.2    Klug, A.3
  • 59
    • 25144476324 scopus 로고    scopus 로고
    • Meiosis-specific yeast Hopl protein promotes pairing of double-stranded DNA helices via G/C isochors
    • Anuradha, S., Tripathi, P., Mahajan, K., and Muniyappa, K. (2005) Meiosis-specific yeast Hopl protein promotes pairing of double-stranded DNA helices via G/C isochors, Biochem. Biophys. Res. Commun. 336, 934-941.
    • (2005) Biochem. Biophys. Res. Commun , vol.336 , pp. 934-941
    • Anuradha, S.1    Tripathi, P.2    Mahajan, K.3    Muniyappa, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.