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Terminase, the DNA packaging enzyme of bacteriophage λ, is a heteromultimer of gpNu1 and gpA subunits. In an earlier investigation, a lethal mutation changing gpA residue 497 from lysine to aspartic acid (K497D) was found to cause a mild change in the high-affinity ATPase that resides in gpA and a severe defect in the endonuclease activity of terminase. The K497D terminase efficiently sponsored packaging...
Terminase, the DNA packaging enzyme of bacteriophage λ, is a heteromultimer composed of gpNu1 (181 aa) and gpA (641 aa) subunits, encoded by the λ Nu1 and A genes, respectively. Similarity between the deduced amino acid sequences of gpNu1 and gpA and the nucleotide binding site consensus sequence suggests that each terminase subunit has an ATP reactive center. Terminase has been shown to have two...
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