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Closed Access item Role of the amino-terminal domain of bacteriophage ø29 connector in DNA binding and packaging

Authors:Donate, L. E.
Valpuesta, José M.
Rocher, A.
Méndez Cormán, Enrique
Rojo, Fernando
Salas, Margarita
Carrascosa, José L.
Issue Date:1992
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
URI:http://hdl.handle.net/10261/38690
ISSN:0021-9258
E-ISSNmetadata.dc.identifier.doi = DOI:1083-351X
Appears in Collections:(CBM) Artículos
(CNB) Artículos

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