Title of article :
Bacteriophage λ Terminase: Alterations of the High-affinity ATPase Affect Viral DNA Packaging Original Research Article
Author/Authors :
Alok Dhar، نويسنده , , Michael Feiss، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Pages :
10
From page :
71
To page :
80
Abstract :
DNA packaging by large DNA viruses such as the tailed bacteriophages and the herpesviruses involves DNA translocation into a preformed protein shell, called the prohead. Translocation is driven by an ATP hydrolysis-powered DNA packaging motor. The bacteriophages encode a heterodimeric viral DNA packaging protein, called terminase. The terminases have an ATPase center located in the N terminus of the large subunit implicated in DNA translocation. In previous work with phage λ, lethal mutations that changed ATP-reactive residues 46 and 84 of gpA, the large terminase subunit, were studied. These mutant enzymes retained the terminase endonuclease and helicase activities, but had severe defects in virion assembly, and lacked the terminase high-affinity ATPase activity.
Keywords :
viral DNA packaging , virus assembly , DNA packaging motor , DNA translocation
Journal title :
Journal of Molecular Biology
Serial Year :
2005
Journal title :
Journal of Molecular Biology
Record number :
692352
Link To Document :
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