참고문헌
-
Mondragon, A., Wolberger, C. and Harrison, S. C. (1989) Structure of phage 434 Cro protein at 2.35
$\AA$ resolution. J. Mol. Biol. 205, 179-188 https://doi.org/10.1016/0022-2836(89)90374-4 -
Ohlendorf, D. H., Tronrud, D. E. and Matthews, B. W. (1998) Refined structure of Cro repressor protein from bacteriophage
$\lambda$ suggests both flexibility and plasticity. J. Mol. Biol. 280,129-136 https://doi.org/10.1006/jmbi.1998.1849 -
LeFevre, K. R. and Cordes, M. H. J. (2003) Retroevolution of
$\lambda$ Cro toward a stable monomer. Proc. Natl. Acad. Sci. U.S.A. 100, 2345-2350 https://doi.org/10.1073/pnas.0537925100 - Newlove, T., Konieczka, J. H. and Cordes, M. H. (2004) Secondary structure switching in Cro protein evolution. Structure. 12, 569-581 https://doi.org/10.1016/j.str.2004.02.024
-
Dubrava, M. S., Ingram, W. M., Roberts, S. A., Weichsel, A., Montfort, W. R. and Cordes, M. H. (2008) N15 Cro and
$\lambda$ Cro: orthologous DNA-binding domains with completely different but equally effective homodimer interfaces. Protein Sci. 17, 803-812 https://doi.org/10.1110/ps.073330808 - Roessler, C. G., Hall, B. M., Anderson, W. J., Ingram, W. M., Roberts, S. A., Montfort, W. R. and Cordes, M. H. (2008) Transitive homology-guided structural studies lead to discovery of Cro proteins with 40% sequence identity but different folds. Proc. Natl. Acad. Sci. U.S.A. 105, 2343-2348 https://doi.org/10.1073/pnas.0711589105
- Gussin, G. N., Sauer, R. T., Pabo, C. R. and Johnson, A. D. (1983) Repressor and Cro protein: Structure, function, and role in lysogenization. In Lambda II (Hendrix, R.W., Roberts, J. W., Stahl, F. W., Weisberg, R.A., eds.) pp. 93- 121, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
-
Iandolo, J. J., Worrell, V., Groicher, K. H., Qian, Y., Tian, R., Kenton, S., Dorman, A., Ji, H., Lin, S., Loh, P., Qi, S., Zhu, H. and Roe, B. A. (2002) Comparative analysis of the genomes of the temperate bacteriophages
$\phi$ 11,$\phi$ 12 and$\phi$ 13 of Staphylococcus aureus 8325. Gene. 289, 109-118 https://doi.org/10.1016/S0378-1119(02)00481-X - Das, M., Ganguly, T., Chattoraj, P., Chanda, P. K., Bandhu, A., Lee, C. Y. and Sau, S. (2007) Purification and characterization of repressor of temperate S. aureus phage phi11. J. Biochem. Mol. Biol. 40, 740-748 https://doi.org/10.5483/BMBRep.2007.40.5.740
- Kenny, J. G., Leach, S., de la Hoz, A. B., Venema, G., Kok, J., Fitzgerald, G. F., Nauta, A., Alonso, J. C. and van Sinderen, D. (2006) Characterization of the lytic-lysogenic switch of the lactococcal bacteriophage Tuc2009. Virology. 347, 434-446 https://doi.org/10.1016/j.virol.2005.11.041
-
Kakikawa, M., Ohkubo, S., Sakate, T., Sayama, M., Taketo, A. and Kodaira, K. (2000) Purification and DNA-binding properties of the cro-type regulatory repressor protein cng encoded by the Lactobacillus plantarum phage
$\phi$ g1e. Gene. 249, 161-169 https://doi.org/10.1016/S0378-1119(00)00146-3 - Ladero, V., Garcia, P., Alonso, J. C. and Suarez, J. E. (2002) Interaction of the Cro repressor with the lysis/lysogeny switch of the Lactobacillus casei temperate bacteriophage A2. J. Gen. Virol. 83, 2891-2895
- Sumby, P. and Waldor, M. K. (2003) Transcription of the toxin genes present within the Staphylococcal phage phiSa3ms is intimately linked with the phage's life cycle. J. Bacteriol. 185, 6841-6851 https://doi.org/10.1128/JB.185.23.6841-6851.2003
- Wolberger, C., Dong, Y. C., Ptashne, M. and Harrison, S. C. (1988) Structure of a phage 434 Cro/DNA complex. Nature. 335, 789-795 https://doi.org/10.1038/335789a0
- Poteete, A. R., Hehir, K. and Sauer, R. T. (1986) Bacteriophage P22 Cro protein: sequence, purification, and properties. Biochemistry. 25, 251-256
- Bushman, F. D. (1993) The bacteriophage 434 right operator. Roles of OR1, OR2 and OR3. J. Mol. Biol. 230, 28-40 https://doi.org/10.1006/jmbi.1993.1123
-
Lee, C.Y. and Iandolo, J. J. (1988) Structural analysis of staphylococcal bacteriophage
$\phi$ 11 attachment sites. J. Bacteriol. 170, 2409-2411 -
Sambrook, J. and Russell, D. W. (2001) In Molecular Cloning: A Laboratory Manual.
$3^{rd}$ ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor , New York - Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K. (1998) In Current Protocols in Molecular Biology, Ch 10, Massachusetts General Hospital, Harvard Medical School, John Wiley & Sons, Inc., U.S.A
- Mandal, P., Chakraborty, P., Sau, S. and Mandal, N. C. (2006) Purification and characterization of a deoxyriboendonuclease from Mycobacterium smegmatis. J. Biochem. Mol. Biol. 39, 140-144 https://doi.org/10.5483/BMBRep.2006.39.2.140
- Ganguly, T., Bandhu, A., Chattoraj, P., Chanda, P. K., Das, M., Mandal, N.C. and Sau, S. (2007) Repressor of temperate mycobacteriophage L1 harbors a stable C-terminal domain and binds to different asymmetric operator DNAs with variable affinity. Virol. J. 4, 64 https://doi.org/10.1186/1743-422X-4-64
- Hecht, M. H., Nelson, H. C. and Sauer, R. T. (1983) Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding. Proc. Natl. Acad. Sci. U.S.A. 80, 2676-2680 https://doi.org/10.1073/pnas.80.9.2676
-
Bandhu, A., Ganguly, T., Chanda, P. K., Das, M. and Sau S (2009)
$Na^+$ and$Mg^{2+}$ have antagonistic effects on the structure, function and stability of repressor of temperate mycobacteriophage L1. BMB Rep. (in press) -
Chanda, P. K., Mondal, R., Sau, K. and S. Sau (2008) Antibiotics, arsenate and
$H_2O_2$ induce the promoter of Staphylococcus aureus cspC gene more strongly than cold. J. Basic Microbiol. 48, 1-7 https://doi.org/10.1002/jobm.200890001 - Koudelka, A. P, Hufnagel, L. A. and Koudelka, G. B. (2004) Purification and characterization of the repressor of the shiga toxin-encoding bacteriophage 933W: DNA binding, gene regulation, and autocleavage. J. Bacteriol. 186, 7659-7669 https://doi.org/10.1128/JB.186.22.7659-7669.2004
- Maxam, A. M. and Gilbert, W. (1980) Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65, 499-560 https://doi.org/10.1016/S0076-6879(80)65059-9
피인용 문헌
- Physicochemical properties and distinct DNA binding capacity of the repressor of temperate Staphylococcus aureus phage φ11 vol.276, pp.7, 2009, https://doi.org/10.1111/j.1742-4658.2009.06924.x
- Insights into aureocin A70 regulation: participation of regulator AurR, alternative transcription factor σB and phage ϕ11 regulator cI vol.167, pp.2, 2016, https://doi.org/10.1016/j.resmic.2015.10.004
- Changes in the Functional Activity of Phi11 Cro Protein is Mediated by Various Ions vol.35, pp.6, 2016, https://doi.org/10.1007/s10930-016-9684-8
- The N-Terminal Domain of the Repressor of Staphylococcus aureus Phage Φ11 Possesses an Unusual Dimerization Ability and DNA Binding Affinity vol.9, pp.4, 2014, https://doi.org/10.1371/journal.pone.0095012
- Characterization of an unusual cold shock protein from Staphylococcus aureus vol.50, pp.6, 2010, https://doi.org/10.1002/jobm.200900264
- Identification and characterization of a CI binding operator at a distant location in the temperate staphylococcal phage ф11 vol.364, pp.20, 2017, https://doi.org/10.1093/femsle/fnx201