Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/38690
Título : Role of the amino-terminal domain of bacteriophage ø29 connector in DNA binding and packaging
Autor : Donate, L. E., Valpuesta, José M., Rocher, A., Méndez Cormán, Enrique, Rojo, Fernando, Salas, Margarita, Carrascosa, José L.
Fecha de publicación : 1992
Editor: American Society for Biochemistry and Molecular Biology
Citación : Journal of Biological Chemistry 267: 10919-10924 (1992)
Resumen: The connector of bacteriophage phi 29 is required for prohead assembly, binds DNA, and drives DNA packaging into viral proheads. Limited proteolysis of the connector protein with endoproteinase Glu-C from Staphylococcus aureus V8 and chymotrypsin showed that a domain of the NH2-terminal region is involved in DNA binding and in the subsequent packaging into preformed proheads, but not in prohead assembly. Mutants in specific amino acids of the NH2-terminal domain, obtained by directed mutagenesis techniques, showed that the Ala1-Arg2-Lys3-Arg4 region of the connector is absolutely necessary for DNA packaging into the proheads as well as for efficient DNA binding.
Versión del editor: http://www.jbc.org/content/267/15/10919.full.pdf+html
URI : http://hdl.handle.net/10261/38690
ISSN: 0021-9258
Citación : Journal of Biological Chemistry 267: 10919-10924 (1992)
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