메뉴 건너뛰기




Volumn 334, Issue 4, 2005, Pages 1233-1240

Protein fragment complementation in M.HhaI DNA methyltransferase

Author keywords

DNA methylation; DNA methyltransferase; Incremental truncation; Leucine zipper; M.AquI; M.BspRI; M.BssHII; M.HhaI; Protein engineering; Protein fragment complementation

Indexed keywords

DNA METHYLTRANSFERASE;

EID: 23044444244     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.07.017     Document Type: Article
Times cited : (20)

References (20)
  • 2
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • S. Klimasauskas, S. Kumar, R.J. Roberts, and X. Cheng HhaI methyltransferase flips its target base out of the DNA helix Cell 76 1994 357 369
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 5
    • 0037096837 scopus 로고    scopus 로고
    • Mutational analysis of conserved residues in HhaI DNA methyltransferase
    • U.T. Sankpal, and D.N. Rao Mutational analysis of conserved residues in HhaI DNA methyltransferase Nucleic Acids Res. 30 2002 2628 2638
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2628-2638
    • Sankpal, U.T.1    Rao, D.N.2
  • 6
    • 0030816214 scopus 로고    scopus 로고
    • Cloning of the BssHII restriction-modification system in Escherichia coli: BssHII methyltransferase contains circularly permuted cytosine-5 methyltransferase motifs
    • S.Y. Xu, J.P. Xiao, J. Posfai, R. Maunus, and J. Benner Cloning of the BssHII restriction-modification system in Escherichia coli: BssHII methyltransferase contains circularly permuted cytosine-5 methyltransferase motifs Nucleic Acids Res. 25 1997 3991
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3991
    • Xu, S.Y.1    Xiao, J.P.2    Posfai, J.3    Maunus, R.4    Benner, J.5
  • 7
    • 0025117570 scopus 로고
    • Agmenellum quadruplicatum M.AquI, a novel modification methylase
    • C. Karreman, and A. deWaard Agmenellum quadruplicatum M.AquI, a novel modification methylase J. Bacteriol. 172 1990 266 272
    • (1990) J. Bacteriol. , vol.172 , pp. 266-272
    • Karreman, C.1    Dewaard, A.2
  • 10
    • 2942564333 scopus 로고    scopus 로고
    • Sequence permutations in the molecular evolution of DNA MTases
    • J.M. Bujnicki Sequence permutations in the molecular evolution of DNA MTases BMC Evol. Biol. 2 2002 3
    • (2002) BMC Evol. Biol. , vol.2 , pp. 3
    • Bujnicki, J.M.1
  • 11
    • 0035997983 scopus 로고    scopus 로고
    • Recombinant alpha and beta subunits of M.AquI constitute an active DNA methyltransferase
    • H. Pinarbasi, E. Pinarbasi, and D. Hornby Recombinant alpha and beta subunits of M.AquI constitute an active DNA methyltransferase J. Biochem. Mol. Biol. 35 2002 348 351
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 348-351
    • Pinarbasi, H.1    Pinarbasi, E.2    Hornby, D.3
  • 12
    • 0026481991 scopus 로고
    • High plasticity of multispecific DNA MTases in the region carrying DNA target recognizing enzyme modules
    • J. Walter, T.A. Trautner, and M. Noyer-Weidner High plasticity of multispecific DNA MTases in the region carrying DNA target recognizing enzyme modules EMBO J. 11 1992 4445 4450
    • (1992) EMBO J. , vol.11 , pp. 4445-4450
    • Walter, J.1    Trautner, T.A.2    Noyer-Weidner, M.3
  • 13
    • 0026757713 scopus 로고
    • How M.MspI and M.HpaII decide which base to methylate
    • S. Mi, and R.J. Roberts How M.MspI and M.HpaII decide which base to methylate Nucleic Acids Res. 20 1992 4811 4816
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4811-4816
    • Mi, S.1    Roberts, R.J.2
  • 15
    • 85080847132 scopus 로고    scopus 로고
    • Enhanced catalytic efficiency of aminoglycoside phosphotransferase (3′)-IIa achieved through protein fragmentation and reassembly
    • (submitted).
    • D.E. Paschon, Z.S. Patel, M. Ostermeier, Enhanced catalytic efficiency of aminoglycoside phosphotransferase (3′)-IIa achieved through protein fragmentation and reassembly, J. Mol. Biol. (submitted).
    • J. Mol. Biol.
    • Paschon, D.E.1    Patel, Z.S.2    Ostermeier, M.3
  • 17
    • 4043054409 scopus 로고    scopus 로고
    • Construction of protein fragment complementation libraries using incremental truncation
    • D. Paschon, and M. Ostermeier Construction of protein fragment complementation libraries using incremental truncation Methods Enzymol. 388 2004 103 116
    • (2004) Methods Enzymol. , vol.388 , pp. 103-116
    • Paschon, D.1    Ostermeier, M.2
  • 19
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein
    • I. Ghosh, A.D. Hamilton, and L. Regan Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein J. Am. Chem. Soc. 122 2000 5658
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5658
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 20
    • 0028956789 scopus 로고
    • Specific DNA-RNA hybrid binding by zinc finger proteins
    • Y. Shi, and J.M. Berg Specific DNA-RNA hybrid binding by zinc finger proteins Science 268 1995 282 284
    • (1995) Science , vol.268 , pp. 282-284
    • Shi, Y.1    Berg, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.