메뉴 건너뛰기




Volumn 45, Issue 10, 2006, Pages 3263-3271

Using offset recombinant polymerase chain reaction to identify functional determinants in a common family of bacterial albumin binding domains

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; GENES; GENETIC ENGINEERING; MUTAGENESIS; THERMODYNAMICS; VIRUSES;

EID: 33644864557     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051926s     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0028341151 scopus 로고
    • Protein PAB, a mosaic albumin-binding bacterial protein representing the first contemporary example of module shuffling
    • de Château, M., and Björck, L. (1994) Protein PAB, a mosaic albumin-binding bacterial protein representing the first contemporary example of module shuffling, J. Biol. Chem. 269, 12147-12151.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12147-12151
    • De Château, M.1    Björck, L.2
  • 3
    • 0028864596 scopus 로고
    • The GA module, a mobile albumin-binding bacterial domain, adopts a three-helix-bundle structure
    • Johansson, M. U., de Château, M., Björck, L., Forsén, S., Drakenberg, T., and Wikström, M. (1995) The GA module, a mobile albumin-binding bacterial domain, adopts a three-helix-bundle structure, FEBS Lett. 374, 257-261.
    • (1995) FEBS Lett. , vol.374 , pp. 257-261
    • Johansson, M.U.1    De Château, M.2    Björck, L.3    Forsén, S.4    Drakenberg, T.5    Wikström, M.6
  • 4
    • 0029970830 scopus 로고    scopus 로고
    • Protein PAB, an albumin-binding bacterial surface protein promoting growth and virulence
    • de Château, M., Holst, E., and Björck, L. (1996) Protein PAB, an albumin-binding bacterial surface protein promoting growth and virulence, J. Biol. Chem. 271, 26609-26615.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26609-26615
    • De Château, M.1    Holst, E.2    Björck, L.3
  • 7
    • 0000137374 scopus 로고
    • In vivo stabilization of a human recombinant CD4-derivate by fusion to a serum-albumin-binding receptor
    • Nygren, P. A., Flodby, P., Andersson, M. U., and Wigzell, H. (1991) In vivo stabilization of a human recombinant CD4-derivate by fusion to a serum-albumin-binding receptor, Vaccines 96, 363-368.
    • (1991) Vaccines , vol.96 , pp. 363-368
    • Nygren, P.A.1    Flodby, P.2    Andersson, M.U.3    Wigzell, H.4
  • 9
    • 0343811733 scopus 로고    scopus 로고
    • The serum albumin-binding region of streptococcal protein G: A bacterial fusion partner with carrier-related properties
    • Sjölander, A., Nygren, P. A., Ståhl, S., Berzins, K., Uhlén, M., Perlmann, P., and Andersson, R. (1997) The serum albumin-binding region of streptococcal protein G: a bacterial fusion partner with carrier-related properties, J. Immunol. Methods 201, 115-123.
    • (1997) J. Immunol. Methods , vol.201 , pp. 115-123
    • Sjölander, A.1    Nygren, P.A.2    Ståhl, S.3    Berzins, K.4    Uhlén, M.5    Perlmann, P.6    Andersson, R.7
  • 10
    • 0033524707 scopus 로고    scopus 로고
    • The serum albumin-binding region of streptococcal protein G (BB) potentiates the immunogenicity of the G130-230 RSV-A protein
    • Libon, C., Corvaia, N., Haeuw, J. F., Nguyen, T. N., Stahl, S., Bonnefoy, J. Y., and Andreoni, C. (1999) The serum albumin-binding region of streptococcal protein G (BB) potentiates the immunogenicity of the G130-230 RSV-A protein, Vaccine 17, 406-414.
    • (1999) Vaccine , vol.17 , pp. 406-414
    • Libon, C.1    Corvaia, N.2    Haeuw, J.F.3    Nguyen, T.N.4    Stahl, S.5    Bonnefoy, J.Y.6    Andreoni, C.7
  • 11
    • 0036304582 scopus 로고    scopus 로고
    • Differences in backbone dynamics of two homologous bacterial albumin-binding modules: Implications for binding specificity and bacterial adaptation
    • Johansson, M. U., Nilsson, H., Evenäs, J., Forsén, S., Drakenberg, T., Björck, L., and Wikström, M. (2002) Differences in backbone dynamics of two homologous bacterial albumin-binding modules: implications for binding specificity and bacterial adaptation, J. Mol. Biol. 316, 1083-1099.
    • (2002) J. Mol. Biol. , vol.316 , pp. 1083-1099
    • Johansson, M.U.1    Nilsson, H.2    Evenäs, J.3    Forsén, S.4    Drakenberg, T.5    Björck, L.6    Wikström, M.7
  • 12
    • 0036145494 scopus 로고    scopus 로고
    • Mutational analysis of the interaction between albumin-binding domain from streptococcal protein G and human serum albumin
    • Linhult, M., Binz, H. K., Uhlén, M., and Hober, S. (2002) Mutational analysis of the interaction between albumin-binding domain from streptococcal protein G and human serum albumin, Protein Sci. 11, 206-213.
    • (2002) Protein Sci. , vol.11 , pp. 206-213
    • Linhult, M.1    Binz, H.K.2    Uhlén, M.3    Hober, S.4
  • 13
    • 0030042286 scopus 로고    scopus 로고
    • The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: A heteronuclear NMR study
    • Kraulis, P. J., Jonasson, P., Nygren, P. A., Uhlén, M., Jendeberg, L., Nilsson, B., and Kördel, J. (1996) The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study, FEBS Lett. 378, 190-194.
    • (1996) FEBS Lett. , vol.378 , pp. 190-194
    • Kraulis, P.J.1    Jonasson, P.2    Nygren, P.A.3    Uhlén, M.4    Jendeberg, L.5    Nilsson, B.6    Kördel, J.7
  • 14
    • 0026661064 scopus 로고
    • Isolation and molecular characterization of a novel albumin-binding protein from group G streptococci
    • Sjobring, U. (1992) Isolation and molecular characterization of a novel albumin-binding protein from group G streptococci, Infect. Immun. 60, 3601-3608.
    • (1992) Infect. Immun. , vol.60 , pp. 3601-3608
    • Sjobring, U.1
  • 15
    • 0343962157 scopus 로고    scopus 로고
    • Stability towards alkaline conditions can be engineered into a protein ligand
    • Gulich, S., Linhult, M., Nygren, P., Uhlén, M., and Hober, S. (2000) Stability towards alkaline conditions can be engineered into a protein ligand, J. Biotechnol. 80, 169-178.
    • (2000) J. Biotechnol. , vol.80 , pp. 169-178
    • Gulich, S.1    Linhult, M.2    Nygren, P.3    Uhlén, M.4    Hober, S.5
  • 16
    • 27844528378 scopus 로고    scopus 로고
    • G148-GA3: A streptococcal virulence module with atypical thermodynamics of folding optimally binds human serum albumin at physiological temperatures
    • Rozak, D. A., Orban, J., and Bryan, P. N. (2005) G148-GA3: A streptococcal virulence module with atypical thermodynamics of folding optimally binds human serum albumin at physiological temperatures, Biochim. Biophys. Acta 1753, 226-233.
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 226-233
    • Rozak, D.A.1    Orban, J.2    Bryan, P.N.3
  • 17
    • 5644272668 scopus 로고    scopus 로고
    • Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin
    • Lejon, S., Frick, I. M., Björck, L., Wikström, M., and Svensson, S. (2004) Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin, J. Biol. Chem. 279, 42924-42928.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42924-42928
    • Lejon, S.1    Frick, I.M.2    Björck, L.3    Wikström, M.4    Svensson, S.5
  • 18
    • 0030858562 scopus 로고    scopus 로고
    • Functional and nonfunctional mutations distinguished by random recombination of homologous genes
    • Zhao, H., and Arnold, F. H. (1997) Functional and nonfunctional mutations distinguished by random recombination of homologous genes, Proc. Natl. Acad. Sci. U.S.A. 94, 7997-8000.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7997-8000
    • Zhao, H.1    Arnold, F.H.2
  • 19
    • 0032814117 scopus 로고    scopus 로고
    • Novel family shuffling methods for the in vitro evolution of enzymes
    • Kikuchi, M., Ohnishi, K., and Harayama, S. (1999) Novel family shuffling methods for the in vitro evolution of enzymes, Gene 236, 159-167.
    • (1999) Gene , vol.236 , pp. 159-167
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 21
    • 0036418698 scopus 로고    scopus 로고
    • Predicting out-of-sequence reassembly in DNA shuffling
    • Moore, G. L., and Maranas, C. D. (2002) Predicting out-of-sequence reassembly in DNA shuffling, J. Theor. Biol. 219, 9-17.
    • (2002) J. Theor. Biol. , vol.219 , pp. 9-17
    • Moore, G.L.1    Maranas, C.D.2
  • 22
    • 0037453068 scopus 로고    scopus 로고
    • Computational and experimental analysis of DNA shuffling
    • Maheshri, N., and Schaffer, D. V. (2003) Computational and experimental analysis of DNA shuffling, Proc. Natl. Acad. Sci. U.S.A. 100, 3071-3076.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3071-3076
    • Maheshri, N.1    Schaffer, D.V.2
  • 23
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. (1994) Rapid evolution of a protein in vitro by DNA shuffling, Nature 370, 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 24
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W. P. (1994) DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution, Proc. Natl. Acad. Sci. U.S.A. 91, 10747-10751.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 25
    • 0033964975 scopus 로고    scopus 로고
    • An effective family shuffling method using single-stranded DNA
    • Kikuchi, M., Ohnishi, K., and Harayama, S. (2000) An effective family shuffling method using single-stranded DNA, Gene 243, 133-137.
    • (2000) Gene , vol.243 , pp. 133-137
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 26
    • 0032850532 scopus 로고    scopus 로고
    • Incremental truncation as a strategy in the engineering of novel biocatalysts
    • Ostermeier, M., Nixon, A. E., and Benkovic, S. J. (1999) Incremental truncation as a strategy in the engineering of novel biocatalysts, Bioorg. Med. Chem. 7, 2139-2144.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 2139-2144
    • Ostermeier, M.1    Nixon, A.E.2    Benkovic, S.J.3
  • 28
    • 0035854021 scopus 로고    scopus 로고
    • Degenerate oligonucleotide gene shuffling (DOGS): A method for enhancing the frequency of recombination with family shuffling
    • Gibbs, M. D., Nevalainen, K. M., and Bergquist, P. L. (2001) Degenerate oligonucleotide gene shuffling (DOGS): a method for enhancing the frequency of recombination with family shuffling, Gene 271, 13-20.
    • (2001) Gene , vol.271 , pp. 13-20
    • Gibbs, M.D.1    Nevalainen, K.M.2    Bergquist, P.L.3
  • 29
    • 27244452777 scopus 로고    scopus 로고
    • Offset recombinant PCR: A simple but effective method for shuffling compact heterologous domains
    • Rozak, D. A., and Bryan, P. N. (2005) Offset recombinant PCR: a simple but effective method for shuffling compact heterologous domains, Nucleic Acids Res. 33, e82.
    • (2005) Nucleic Acids Res. , vol.33
    • Rozak, D.A.1    Bryan, P.N.2
  • 30
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H. R., Griffiths, A. D., Johnson, K. S., Chiswell, D. J., Hudson, P., and Winter, G. (1991) Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains, Nucleic Acids Res. 19, 4133-4137.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 31
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange site-directed mutagenesis
    • Wang, W., and Malcolm, B. A. (1999) Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange site-directed mutagenesis, BioTechniques 26, 680-682.
    • (1999) BioTechniques , vol.26 , pp. 680-682
    • Wang, W.1    Malcolm, B.A.2
  • 32
    • 8744294716 scopus 로고    scopus 로고
    • Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification
    • Ruan, B., Fisher, K. E., Alexander, P. A., Doroshko, V., and Bryan, P. N. (2004) Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification, Biochemistry 43, 14539-14546.
    • (2004) Biochemistry , vol.43 , pp. 14539-14546
    • Ruan, B.1    Fisher, K.E.2    Alexander, P.A.3    Doroshko, V.4    Bryan, P.N.5
  • 33
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.