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Volumn 319, Issue 3, 2002, Pages 673-683

Directed evolution of restriction endonuclease BstYI to achieve increased substrate specificity

Author keywords

BstYI; DNA methyltransferase; Endonuclease substrate specificity; Protein evolution; Restriction endonuclease

Indexed keywords

CELL DNA; DNA METHYLTRANSFERASE; RESTRICTION ENDONUCLEASE;

EID: 0036304570     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00343-1     Document Type: Article
Times cited : (42)

References (32)
  • 3
    • 0031970935 scopus 로고    scopus 로고
    • Mutational analysis of the function of Met137 and Ile197, two amino acids implicated in sequence-specific DNA recognition by the EcoRI endonuclease
    • (1998) Biol. Chem. , vol.379 , pp. 459-465
    • Ivanenko, T.1    Heitman, J.2    Kiss, A.3
  • 9
    • 0024589458 scopus 로고
    • Changing the hydrogen-bonding potential in the DNA binding site of EcoRI by site-directed mutagenesis drastically reduces the enzymatic activity, not, however, the preference of this restriction endonuclease for cleavage within the site-GAATTC-
    • (1989) Biochemistry , vol.28 , pp. 2678-2684
    • Alves, J.1    Ruter, T.2    Geiger, R.3    Fleiss, A.4    Maass, G.5    Pingoud, A.6
  • 10
    • 0032555574 scopus 로고    scopus 로고
    • Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts
    • (1998) J. Biol. Chem. , vol.273 , pp. 21721-21729
    • Horton, N.C.1    Perona, J.J.2
  • 11
    • 0034026486 scopus 로고    scopus 로고
    • On the possibilities and limitations of rational protein design to expand the specificity of restriction enzymes: A case study employing EcoRV as the target
    • (2000) Protein Eng. , vol.13 , pp. 275-281
    • Lanio, T.1    Jeltsch, A.2    Pingoud, A.3
  • 12
    • 0032538280 scopus 로고    scopus 로고
    • Towards the design of rare cutting restriction endonucleases: Using directed evolution to generate variants of EcoRV differing in their substrate specificity by two orders of magnitude
    • (1998) J. Mol. Biol. , vol.283 , pp. 59-69
    • Lanio, T.1    Jeltsch, A.2    Pingoud, A.3
  • 13
    • 0025171673 scopus 로고
    • Mutants of the EcoRI endonuclease with promiscuous substrate specificity implicate residues involved in substrate recognition
    • (1990) EMBO J. , vol.9 , pp. 3369-3378
    • Heitman, J.1    Model, P.2
  • 15
    • 0026898962 scopus 로고
    • How the EcoRI endonuclease recognizes and cleaves DNA
    • (1992) BioEssays , vol.14 , pp. 445-454
    • Heitman, J.1
  • 19
  • 20
    • 0021320685 scopus 로고
    • Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli
    • (1984) Microbiol. Rev. , vol.48 , pp. 60-93
    • Walker, G.C.1
  • 27
    • 0031576347 scopus 로고    scopus 로고
    • Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis
    • (1997) J. Mol. Biol. , vol.273 , pp. 207-225
    • Perona, J.J.1    Martin, A.M.2
  • 28
    • 0032502924 scopus 로고    scopus 로고
    • Role of protein-induced bending in the specificity of DNA recognition: Crystal structure of EcoRV endonuclease complexed with d(AAAGAT) + d(ATCTT)
    • (1998) J. Mol. Biol. , vol.277 , pp. 779-787
    • Horton, N.C.1    Perona, J.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.