Role of the amino-terminal domain of bacteriophage phi 29 connector in DNA binding and packaging. |
| |
| Authors: | L E Donate J M Valpuesta A Rocher E Méndez F Rojo M Salas J L Carrascosa |
| |
| Institution: | Centro de Biología Molecular, Universidad Autónoma de Madrid, Spain. |
| |
| 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. |
| |
| Keywords: | |
|
|
