Mutations abolishing the endonuclease activity of bacteriophage lambda terminase lie in two distinct regions of the A gene, one of which may encode a "leucine zipper" DNA-binding domain.

Abstract excerpt

Bacteriophage lambda terminase is a multifunctional enzyme composed of two subunits which are the products of the phage-encoded Nu1 and A genes. The enzyme catalyzes the endonucleolytic cleavage of lambda DNA at a site known as cosN and mediates packaging of the phage DNA into empty heads. This work describes the characterization of mutations within the A gene which lead to the loss of terminase endonuclease...

Topics

• Amino Acid Sequence
• Bacteriophage lambda
• DNA Mutational Analysis
• DNA Primase
• DNA-Directed DNA Polymerase
• Endodeoxyribonucleases
• Genes, Viral
• Leucine Zippers
• Molecular Sequence Data
• Mutation