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- W4291021411 endingPage "8732" @default.
- W4291021411 startingPage "8719" @default.
- W4291021411 abstract "Abstract Many essential cellular processes rely on substrate rotation or translocation by a multi-subunit, ring-type NTPase. A large number of double-stranded DNA viruses, including tailed bacteriophages and herpes viruses, use a homomeric ring ATPase to processively translocate viral genomic DNA into procapsids during assembly. Our current understanding of viral DNA packaging comes from three archetypal bacteriophage systems: cos, pac and phi29. Detailed mechanistic understanding exists for pac and phi29, but not for cos. Here, we reconstituted in vitro a cos packaging system based on bacteriophage HK97 and provided a detailed biochemical and structural description. We used a photobleaching-based, single-molecule assay to determine the stoichiometry of the DNA-translocating ATPase large terminase. Crystal structures of the large terminase and DNA-recruiting small terminase, a first for a biochemically defined cos system, reveal mechanistic similarities between cos and pac systems. At the same time, mutational and biochemical analyses indicate a new regulatory mechanism for ATPase multimerization and coordination in the HK97 system. This work therefore establishes a framework for studying the evolutionary relationships between ATP-dependent DNA translocation machineries in double-stranded DNA viruses." @default.
- W4291021411 created "2022-08-13" @default.
- W4291021411 creator A5000773425 @default.
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- W4291021411 date "2022-08-10" @default.
- W4291021411 modified "2023-10-11" @default.
- W4291021411 title "Structural basis of DNA packaging by a ring-type ATPase from an archetypal viral system" @default.
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