메뉴 건너뛰기




Volumn 377, Issue 3, 2008, Pages 862-866

Mutational analysis and a structural model of methyl-directed restriction enzyme Mrr

Author keywords

Escherichia coli; High pressure; Mrr; Mutagenesis; Protein modeling; Restriction

Indexed keywords

PROTEIN MRR; RESTRICTION ENDONUCLEASE; UNCLASSIFIED DRUG;

EID: 56249121930     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.10.064     Document Type: Article
Times cited : (11)

References (32)
  • 1
    • 22544464152 scopus 로고    scopus 로고
    • The biology of restriction and antirestriction
    • Tock M.R., and Dryden D.T. The biology of restriction and antirestriction. Curr. Opin. Microbiol. 8 (2005) 466-472
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 466-472
    • Tock, M.R.1    Dryden, D.T.2
  • 2
    • 33646008874 scopus 로고    scopus 로고
    • N6-methyl-adenine: an epigenetic signal for DNA-protein interactions
    • Wion D., and Casadesus J. N6-methyl-adenine: an epigenetic signal for DNA-protein interactions. Nat. Rev. Microbiol. 4 (2006) 183-192
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 183-192
    • Wion, D.1    Casadesus, J.2
  • 4
    • 0035876202 scopus 로고    scopus 로고
    • The McrBC restriction endonuclease assembles into a ring structure in the presence of G nucleotides
    • Panne D., Muller S.A., Wirtz S., Engel A., and Bickle T.A. The McrBC restriction endonuclease assembles into a ring structure in the presence of G nucleotides. EMBO J. 20 (2001) 3210-3217
    • (2001) EMBO J. , vol.20 , pp. 3210-3217
    • Panne, D.1    Muller, S.A.2    Wirtz, S.3    Engel, A.4    Bickle, T.A.5
  • 5
    • 0033822258 scopus 로고    scopus 로고
    • Atomic model of the 5-methylcytosine-specific restriction enzyme McrA reveals an atypical zinc finger and structural similarity to betabetaalphaMe endonucleases
    • Bujnicki J.M., Radlinska M., and Rychlewski L. Atomic model of the 5-methylcytosine-specific restriction enzyme McrA reveals an atypical zinc finger and structural similarity to betabetaalphaMe endonucleases. Mol. Microbiol. 37 (2000) 1280-1281
    • (2000) Mol. Microbiol. , vol.37 , pp. 1280-1281
    • Bujnicki, J.M.1    Radlinska, M.2    Rychlewski, L.3
  • 6
    • 4344643339 scopus 로고    scopus 로고
    • Transposon-mediated linker insertion scanning mutagenesis of the Escherichia coli McrA endonuclease
    • Anton B.P., and Raleigh E.A. Transposon-mediated linker insertion scanning mutagenesis of the Escherichia coli McrA endonuclease. J. Bacteriol. 186 (2004) 5699-5707
    • (2004) J. Bacteriol. , vol.186 , pp. 5699-5707
    • Anton, B.P.1    Raleigh, E.A.2
  • 7
    • 0035906281 scopus 로고    scopus 로고
    • Identification of a PD-(D/E)XK-like domain with a novel configuration of the endonuclease active site in the methyl-directed restriction enzyme Mrr and its homologs
    • Bujnicki J.M., and Rychlewski L. Identification of a PD-(D/E)XK-like domain with a novel configuration of the endonuclease active site in the methyl-directed restriction enzyme Mrr and its homologs. Gene 267 (2001) 183-191
    • (2001) Gene , vol.267 , pp. 183-191
    • Bujnicki, J.M.1    Rychlewski, L.2
  • 8
    • 0023274383 scopus 로고
    • Site-specific methylases induce the SOS DNA repair response in Escherichia coli
    • Heitman J., and Model P. Site-specific methylases induce the SOS DNA repair response in Escherichia coli. J. Bacteriol. 169 (1987) 3243-3250
    • (1987) J. Bacteriol. , vol.169 , pp. 3243-3250
    • Heitman, J.1    Model, P.2
  • 9
    • 4444274584 scopus 로고    scopus 로고
    • An SOS response induced by high pressure in Escherichia coli
    • Aertsen A., Van Houdt R., Vanoirbeek K., and Michiels C.W. An SOS response induced by high pressure in Escherichia coli. J. Bacteriol. 186 (2004) 6133-6141
    • (2004) J. Bacteriol. , vol.186 , pp. 6133-6141
    • Aertsen, A.1    Van Houdt, R.2    Vanoirbeek, K.3    Michiels, C.W.4
  • 10
    • 28244432478 scopus 로고    scopus 로고
    • Mrr instigates the SOS response after high pressure stress in Escherichia coli
    • Aertsen A., and Michiels C.W. Mrr instigates the SOS response after high pressure stress in Escherichia coli. Mol. Microbiol. 58 (2005) 1381-1391
    • (2005) Mol. Microbiol. , vol.58 , pp. 1381-1391
    • Aertsen, A.1    Michiels, C.W.2
  • 11
    • 46949087594 scopus 로고    scopus 로고
    • Using mild high-pressure shock to generate bacterial ghosts of Escherichia coli
    • Vanlint D., Mebrhatu Tesfazgi M., Michiels C.W., and Aertsen A. Using mild high-pressure shock to generate bacterial ghosts of Escherichia coli. Z. Naturforsch. B 63b (2008) 765-768
    • (2008) Z. Naturforsch. B , vol.63 b , pp. 765-768
    • Vanlint, D.1    Mebrhatu Tesfazgi, M.2    Michiels, C.W.3    Aertsen, A.4
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko K.A., and Wanner B.L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97 (2000) 6640-6645
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0025325983 scopus 로고
    • The megaprimer. Method of site-directed mutagenesis
    • Sarkar G., and Sommer S.S. The megaprimer. Method of site-directed mutagenesis. Biotechniques 8 (1990) 404-407
    • (1990) Biotechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 15
    • 10044222704 scopus 로고    scopus 로고
    • CLANS: a Java application for visualizing protein families based on pairwise similarity
    • Frickey T., and Lupas A. CLANS: a Java application for visualizing protein families based on pairwise similarity. Bioinformatics 20 (2004) 3702-3704
    • (2004) Bioinformatics , vol.20 , pp. 3702-3704
    • Frickey, T.1    Lupas, A.2
  • 16
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K., Misawa K., Kuma K., and Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 30 (2002) 3059-3066
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 17
    • 0043123216 scopus 로고    scopus 로고
    • GeneSilico protein structure prediction meta-server
    • Kurowski M.A., and Bujnicki J.M. GeneSilico protein structure prediction meta-server. Nucleic Acids Res. 31 (2003) 3305-3307
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 18
    • 0034780030 scopus 로고    scopus 로고
    • Pcons: a neural-network-based consensus predictor that improves fold recognition
    • Lundstrom J., Rychlewski L., Bujnicki J., and Elofsson A. Pcons: a neural-network-based consensus predictor that improves fold recognition. Protein Sci. 10 (2001) 2354-2362
    • (2001) Protein Sci. , vol.10 , pp. 2354-2362
    • Lundstrom, J.1    Rychlewski, L.2    Bujnicki, J.3    Elofsson, A.4
  • 19
    • 0242362160 scopus 로고    scopus 로고
    • A "FRankenstein's monster" approach to comparative modeling: merging the finest fragments of fold-recognition models and iterative model refinement aided by 3D structure evaluation
    • Kosinski J., Cymerman I.A., Feder M., Kurowski M.A., Sasin J.M., and Bujnicki J.M. A "FRankenstein's monster" approach to comparative modeling: merging the finest fragments of fold-recognition models and iterative model refinement aided by 3D structure evaluation. Proteins 53 Suppl. 6 (2003) 369-379
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 369-379
    • Kosinski, J.1    Cymerman, I.A.2    Feder, M.3    Kurowski, M.A.4    Sasin, J.M.5    Bujnicki, J.M.6
  • 21
    • 0242330730 scopus 로고    scopus 로고
    • Assessment of homology-based predictions in CASP5
    • Tramontano A., and Morea V. Assessment of homology-based predictions in CASP5. Proteins 53 Suppl. 6 (2003) 352-368
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 352-368
    • Tramontano, A.1    Morea, V.2
  • 22
    • 30344449457 scopus 로고    scopus 로고
    • Assessment of fold recognition predictions in CASP6
    • Wang G., Jin Y., and Dunbrack Jr. R.L. Assessment of fold recognition predictions in CASP6. Proteins 61 Suppl. 7 (2005) 46-66
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 46-66
    • Wang, G.1    Jin, Y.2    Dunbrack Jr., R.L.3
  • 23
    • 34249866596 scopus 로고    scopus 로고
    • A model of restriction endonuclease MvaI in complex with DNA: a template for interpretation of experimental data and a guide for specificity engineering
    • Kosinski J., Kubareva E., and Bujnicki J.M. A model of restriction endonuclease MvaI in complex with DNA: a template for interpretation of experimental data and a guide for specificity engineering. Proteins 68 (2007) 324-336
    • (2007) Proteins , vol.68 , pp. 324-336
    • Kosinski, J.1    Kubareva, E.2    Bujnicki, J.M.3
  • 24
    • 34047130851 scopus 로고    scopus 로고
    • I-Ssp6803I: the first homing endonuclease from the PD-(D/E)XK superfamily exhibits an unusual mode of DNA recognition
    • Orlowski J., Boniecki M., and Bujnicki J.M. I-Ssp6803I: the first homing endonuclease from the PD-(D/E)XK superfamily exhibits an unusual mode of DNA recognition. Bioinformatics 23 (2007) 527-530
    • (2007) Bioinformatics , vol.23 , pp. 527-530
    • Orlowski, J.1    Boniecki, M.2    Bujnicki, J.M.3
  • 25
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons K.T., Kooperberg C., Huang E., and Baker D. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268 (1997) 209-225
    • (1997) J. Mol. Biol. , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 26
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 27
    • 0037406141 scopus 로고    scopus 로고
    • Can correct protein models be identified?
    • Wallner B., and Elofsson A. Can correct protein models be identified?. Protein Sci. 12 (2003) 1073-1086
    • (2003) Protein Sci. , vol.12 , pp. 1073-1086
    • Wallner, B.1    Elofsson, A.2
  • 28
    • 54949097750 scopus 로고    scopus 로고
    • MetaMQAP: a meta-server for the quality assessment of protein models
    • Pawlowski M., Gajda M.J., Matlak R., and Bujnicki J.M. MetaMQAP: a meta-server for the quality assessment of protein models. BMC Bioinformatics 9 (2008) 403
    • (2008) BMC Bioinformatics , vol.9 , pp. 403
    • Pawlowski, M.1    Gajda, M.J.2    Matlak, R.3    Bujnicki, J.M.4
  • 29
    • 25444522883 scopus 로고    scopus 로고
    • The PD-(D/E)XK superfamily revisited: identification of new members among proteins involved in DNA metabolism and functional predictions for domains of (hitherto) unknown function
    • Kosinski J., Feder M., and Bujnicki J.M. The PD-(D/E)XK superfamily revisited: identification of new members among proteins involved in DNA metabolism and functional predictions for domains of (hitherto) unknown function. BMC Bioinformatics 6 (2005) 172
    • (2005) BMC Bioinformatics , vol.6 , pp. 172
    • Kosinski, J.1    Feder, M.2    Bujnicki, J.M.3
  • 30
    • 0027275485 scopus 로고
    • The winged-helix DNA-binding motif: another helix-turn-helix takeoff
    • Brennan R.G. The winged-helix DNA-binding motif: another helix-turn-helix takeoff. Cell 74 (1993) 773-776
    • (1993) Cell , vol.74 , pp. 773-776
    • Brennan, R.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.