Abstract:
:Double-stranded DNA viruses use ATP-powered molecular motors to package their genomic DNA. To ensure efficient genome encapsidation, these motors regulate functional transitions between initiation, translocation, and termination modes. Here, we report structural and biophysical analyses of the C-terminal domain of the bacteriophage phi29 ATPase (CTD) that suggest a structural basis for these functional transitions. Sedimentation experiments show that the inter-domain linker in the full-length protein promotes oligomerization and thus may play a role in assembly of the functional motor. The NMR solution structure of the CTD indicates it is a vestigial nuclease domain that likely evolved from conserved nuclease domains in phage terminases. Despite the loss of nuclease activity, fluorescence binding assays confirm the CTD retains its DNA binding capabilities and fitting the CTD into cryoEM density of the phi29 motor shows that the CTD directly binds DNA. However, the interacting residues differ from those identified by NMR titration in solution, suggesting that packaging motors undergo conformational changes to transition between initiation, translocation, and termination. Taken together, these results provide insight into the evolution of functional transitions in viral dsDNA packaging motors.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Mahler BP,Bujalowski PJ,Mao H,Dill EA,Jardine PJ,Choi KH,Morais MCdoi
10.1093/nar/gkaa874subject
Has Abstractpub_date
2020-11-18 00:00:00pages
11737-11749issue
20eissn
0305-1048issn
1362-4962pii
5934415journal_volume
48pub_type
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