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Masai, H., Arai, K. (1987) RepA and DnaA proteins are required for initiation of R1 plasmid replication in vitro and interact with the oriR sequence. Proceedings of the National Academy of Sciences, 84 (14) 4781-4785 doi:10.1073/pnas.84.14.4781

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Reference TypeJournal (article/letter/editorial)
TitleRepA and DnaA proteins are required for initiation of R1 plasmid replication in vitro and interact with the oriR sequence.
JournalProceedings of the National Academy of Sciences
AuthorsMasai, H.Author
Arai, K.Author
Year1987 (July 1)Volume84
Issue14
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.84.14.4781Search in ResearchGate
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Mindat Ref. ID1458991Long-form Identifiermindat:1:5:1458991:5
GUID0
Full ReferenceMasai, H., Arai, K. (1987) RepA and DnaA proteins are required for initiation of R1 plasmid replication in vitro and interact with the oriR sequence. Proceedings of the National Academy of Sciences, 84 (14) 4781-4785 doi:10.1073/pnas.84.14.4781
Plain TextMasai, H., Arai, K. (1987) RepA and DnaA proteins are required for initiation of R1 plasmid replication in vitro and interact with the oriR sequence. Proceedings of the National Academy of Sciences, 84 (14) 4781-4785 doi:10.1073/pnas.84.14.4781
In(1987, July) Proceedings of the National Academy of Sciences Vol. 84 (14) Proceedings of the National Academy of Sciences

See Also

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Masai, H., Kaziro, Y., Arai, K. (1983) Definition of oriR, the minimum DNA segment essential for initiation of R1 plasmid replication in vitro. Proceedings of the National Academy of Sciences, 80 (22) 6814-6818 doi:10.1073/pnas.80.22.6814
Wickner, S. H., Chattoraj, D. K. (1987) Replication of mini-P1 plasmid DNA in vitro requires two initiation proteins, encoded by the repA gene of phage P1 and the dnaA gene of Escherichia coli. Proceedings of the National Academy of Sciences, 84 (11) 3668-3672 doi:10.1073/pnas.84.11.3668
Giraldo, Rafael, Díaz, Ramón (1992) Differential binding of wild-type and a mutant RepA protein to oriR sequence suggests a model for the initiation of plasmid R1 replication. Journal of Molecular Biology, 228 (3). 787-802 doi:10.1016/0022-2836(92)90864-g
Wickner, S., Skowyra, D., Hoskins, J., McKenney, K. (1992) DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step. Proceedings of the National Academy of Sciences, 89 (21) 10345-10349 doi:10.1073/pnas.89.21.10345
Boye, E., Stokke, T., Kleckner, N., Skarstad, K. (1996) Coordinating DNA replication initiation with cell growth: differential roles for DnaA and SeqA proteins. Proceedings of the National Academy of Sciences, 93 (22) 12206-12211 doi:10.1073/pnas.93.22.12206
Manen, D., Upegui-Gonzalez, L. C., Caro, L. (1992) Monomers and dimers of the RepA protein in plasmid pSC101 replication: domains in RepA. Proceedings of the National Academy of Sciences, 89 (19) 8923-8927 doi:10.1073/pnas.89.19.8923
Wickner, S. H. (1990) Three Escherichia coli heat shock proteins are required for P1 plasmid DNA replication: formation of an active complex between E. coli DnaJ protein and the P1 initiator protein. Proceedings of the National Academy of Sciences, 87 (7) 2690-2694 doi:10.1073/pnas.87.7.2690
Kasho, K., Katayama, T. (2013) DnaA binding locus datA promotes DnaA-ATP hydrolysis to enable cell cycle-coordinated replication initiation. Proceedings of the National Academy of Sciences, 110 (3) 936-941 doi:10.1073/pnas.1212070110
Tsurimoto, T., Matsubara, K. (1982) Replication of lambda dv plasmid in vitro promoted by purified lambda O and P proteins. Proceedings of the National Academy of Sciences, 79 (24) 7639-7643 doi:10.1073/pnas.79.24.7639
Gruss, A. D., Ross, H. F., Novick, R. P. (1987) Functional analysis of a palindromic sequence required for normal replication of several staphylococcal plasmids. Proceedings of the National Academy of Sciences, 84 (8) 2165-2169 doi:10.1073/pnas.84.8.2165
Chattoraj, D. K., Snyder, K. M., Abeles, A. L. (1985) P1 plasmid replication: multiple functions of RepA protein at the origin. Proceedings of the National Academy of Sciences, 82 (9) 2588-2592 doi:10.1073/pnas.82.9.2588
 
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