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|Title:||Role of the amino-terminal domain of bacteriophage ø29 connector in DNA binding and packaging|
|Authors:||Donate, L. E.; Valpuesta, José M.; Rocher, Asunción ; Méndez Cormán, Enrique; Rojo, Fernando; Salas, Margarita; Carrascosa, José L.|
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Citation:||Journal of Biological Chemistry 267: 10919-10924 (1992)|
|Abstract:||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.|
|Publisher version (URL):||http://www.jbc.org/content/267/15/10919.full.pdf+html|
|Appears in Collections:||(CBM) Artículos|
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