Abstract
The Arc and Mnt repressors of phage P22 are related proteins that bind to different operator DNA sites. By creating a hybrid Arc-Mnt protein, we show that the binding specificity of Mnt can be switched to that of Arc by replacing six residues at the N terminus of Mnt with the corresponding nine residues from Arc.
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- Amann E., Brosius J., Ptashne M. Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli. Gene. 1983 Nov;25(2-3):167–178. doi: 10.1016/0378-1119(83)90222-6. [DOI] [PubMed] [Google Scholar]
- Anderson J. E., Ptashne M., Harrison S. C. Structure of the repressor-operator complex of bacteriophage 434. 1987 Apr 30-May 6Nature. 326(6116):846–852. doi: 10.1038/326846a0. [DOI] [PubMed] [Google Scholar]
- Botstein K., Lew K. K., Jarvik V., Swanson C. A. Role of antirepressor in the bipartite control of repression and immunity by bacteriophage P22. J Mol Biol. 1975 Feb 5;91(4):439–462. doi: 10.1016/0022-2836(75)90271-5. [DOI] [PubMed] [Google Scholar]
- Fried M., Crothers D. M. Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis. Nucleic Acids Res. 1981 Dec 11;9(23):6505–6525. doi: 10.1093/nar/9.23.6505. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Garner M. M., Revzin A. A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system. Nucleic Acids Res. 1981 Jul 10;9(13):3047–3060. doi: 10.1093/nar/9.13.3047. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Knight K. L., Sauer R. T. The Mnt repressor of bacteriophage P22: role of C-terminal residues in operator binding and tetramer formation. Biochemistry. 1988 Mar 22;27(6):2088–2094. doi: 10.1021/bi00406a041. [DOI] [PubMed] [Google Scholar]
- Sauer R. T., Krovatin W., DeAnda J., Youderian P., Susskind M. M. Primary structure of the immI immunity region of bacteriophage P22. J Mol Biol. 1983 Aug 25;168(4):699–713. doi: 10.1016/s0022-2836(83)80070-9. [DOI] [PubMed] [Google Scholar]
- Tullius T. D., Dombroski B. A. Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein. Proc Natl Acad Sci U S A. 1986 Aug;83(15):5469–5473. doi: 10.1073/pnas.83.15.5469. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vershon A. K., Bowie J. U., Karplus T. M., Sauer R. T. Isolation and analysis of arc repressor mutants: evidence for an unusual mechanism of DNA binding. Proteins. 1986 Dec;1(4):302–311. doi: 10.1002/prot.340010404. [DOI] [PubMed] [Google Scholar]
- Vershon A. K., Liao S. M., McClure W. R., Sauer R. T. Bacteriophage P22 Mnt repressor. DNA binding and effects on transcription in vitro. J Mol Biol. 1987 May 20;195(2):311–322. doi: 10.1016/0022-2836(87)90652-8. [DOI] [PubMed] [Google Scholar]
- Vershon A. K., Liao S. M., McClure W. R., Sauer R. T. Interaction of the bacteriophage P22 Arc repressor with operator DNA. J Mol Biol. 1987 May 20;195(2):323–331. doi: 10.1016/0022-2836(87)90653-x. [DOI] [PubMed] [Google Scholar]
- Vershon A. K., Youderian P., Susskind M. M., Sauer R. T. The bacteriophage P22 arc and mnt repressors. Overproduction, purification, and properties. J Biol Chem. 1985 Oct 5;260(22):12124–12129. [PubMed] [Google Scholar]
- Wharton R. P., Ptashne M. Changing the binding specificity of a repressor by redesigning an alpha-helix. Nature. 1985 Aug 15;316(6029):601–605. doi: 10.1038/316601a0. [DOI] [PubMed] [Google Scholar]
- Youderian P., Vershon A., Bouvier S., Sauer R. T., Susskind M. M. Changing the DNA-binding specificity of a repressor. Cell. 1983 Dec;35(3 Pt 2):777–783. doi: 10.1016/0092-8674(83)90110-1. [DOI] [PubMed] [Google Scholar]