참고문헌
- Berger, N., Heller, A. E., Stormann, K. D. and Pfaff, E. (2001) Characterization of chimeric enzymes between caprine arthritisencephaltis virus, maedi-visna virus and human immunodeficiency virus type 1 intergrases expressed in E. coli. J. Gen. Virol. 82, 139-148. https://doi.org/10.1099/0022-1317-82-1-139
- Brown, J. E., Klement, J. F. and MacAllister, W. T. (1986) Sequences of three promoters for the bacteriophage SP6 RNA polymerase. Nucleic Acids Res. 14, 3521-3526. https://doi.org/10.1093/nar/14.8.3521
- Chamberlin, M., McGrath, J. and Waskell, L. (1970) New RNA polymerase from Escherichia coli infected with baceriophage T7. Nature 228, 227-231. https://doi.org/10.1038/228227a0
- Cheng, X., Zhang, X., Pflugrath, J. W. and Studier, F. W. (1993) The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Proc. Natl. Acad. Sci. 91, 4034-4038.
- Clark, E. D. (1998) Refolding of recombinant proteins. Curr. Opinion Biotech. 9, 157-163. https://doi.org/10.1016/S0958-1669(98)80109-2
- Dietz, A., Weisser, H.-J., Kossel, H. and Hausmann, R. (1990) The gene for Klebsiella bacteriophage K11 RNA polymerase: Sequence and comparison with the homologous genes of phages T7, T3, and SP6. Mol. Gen. Genet. 221, 283-286.
- Dunn, J. J. and Studier, F. W. (1983) Complete nucleotide sequence of bacteriophage T7 DNA and locations of T7 genetic elements. J. Mol. Biol. 166, 477-535 https://doi.org/10.1016/S0022-2836(83)80282-4
- Han, K. G., Lee, S. S. and Kang, C. (1999) Soluble expression of cloned phage K11 RNA polymerase gene in Escherichia coli at a low temperature. Protein Express. Purif. 16, 103-108. https://doi.org/10.1006/prep.1999.1061
- Han, K. G., Kim, D. H., Junn, E., Lee, S. S. and Kang, C. (2002) Identification of bacteriophage K11 genomic promoters for K11 RNA polymerase. J. Biochem. Mol. Biol. 35, 637-641. https://doi.org/10.5483/BMBRep.2002.35.6.637
- Huang, J., Villemain, J., Padilla, R. and Sousa, R. (1999) Mechanisms by which T7 lysozyme specifically regulates T7 RNA polymerase during different phases of transcription. J. Mol. Biol. 293, 457-475. https://doi.org/10.1006/jmbi.1999.3135
- Ikeda, R. A. and Bailey, P. A. (1992) Inhibition of T7 RNA polymerase by T7 lysozyme in vitro. J. Biol. Chem. 267, 20153-20158.
- Inouye, M., Arnheim, N. and Sternglanz, R. (1973) Bacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase. J. Biol. Chem. 25, 7247-7252.
- Jeruzalmi, D. and Steitz, T. A. (1998) Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. EMBO 17, 4101-4113. https://doi.org/10.1093/emboj/17.14.4101
- Junn, H. J., Youn, J., Suh, K. H. and Lee, S. S. (2005) Cloning and expression of Klebsiella phage K11 lysozyme gene. Protein Express. Purif. 42, 78-84. https://doi.org/10.1016/j.pep.2005.03.026
- Moffatt, B. A. and Studier, F. W. (1987) T7 lysozyme inhibits transcription by T7 RNA polymerase. Cell 49, 221-227. https://doi.org/10.1016/0092-8674(87)90563-0
- Rosa, M. D. and Andrews, N. C. (1981) Phage T3 DNA contains an extra copy of 23 base-pair phage T7 RNA polymerase promoter sequence. J. Mol. Biol. 147, 41-53. https://doi.org/10.1016/0022-2836(81)90078-4
-
Singh, A. and Hayashi, K. (1995) Construction of chimeric
${\beta}-glucosidases$ with improved enzymatic properties. J. Biol. Chem. 270, 21928-21933. https://doi.org/10.1074/jbc.270.37.21928 - Terpe, K. (2003) Overview of tag protein fusions: from molecules and biochemical fundamentals to commercial systems. Appli. Microbiol. Biotechnol. 60, 523-533. https://doi.org/10.1007/s00253-002-1158-6
- Zhang, X. and Studier, F. W. (1995) Isolation of transcriptionally active mutants of T7 RNA polymerase that do not support phage growth. J. Mol. Biol. 250, 156-168. https://doi.org/10.1006/jmbi.1995.0367
- Zhang, X. and Studier, F. W. (2004) Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage T7 infection. J. Mol. Biol. 340, 707-730. https://doi.org/10.1016/j.jmb.2004.05.006
피인용 문헌
- Role of Net Charge on Catalytic Domain and Influence of Cell Wall Binding Domain on Bactericidal Activity, Specificity, and Host Range of Phage Lysins vol.286, pp.39, 2011, https://doi.org/10.1074/jbc.M111.244160
- Elucidating the pH-Dependent Structural Transition of T7 Bacteriophage Endolysin vol.55, pp.33, 2016, https://doi.org/10.1021/acs.biochem.6b00240
- Recombinant bacteriophage lysins as antibacterials vol.1, pp.1, 2010, https://doi.org/10.4161/bbug.1.1.9818
- Domain function dissection and catalytic properties of Listeria monocytogenes p60 protein with bacteriolytic activity vol.99, pp.24, 2015, https://doi.org/10.1007/s00253-015-6967-5
- 3DSwap: curated knowledgebase of proteins involved in 3D domain swapping vol.2011, pp.0, 2011, https://doi.org/10.1093/database/bar042