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TitleA thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry.
Journal, issue, pagesJ Biol Chem, Vol. 295, Issue 12, Page 3783-3793, Year 2020
Publish dateMar 20, 2020
AuthorsJanelle A Hayes / Brendan J Hilbert / Christl Gaubitz / Nicholas P Stone / Brian A Kelch /
PubMed AbstractTailed bacteriophages use a DNA-packaging motor to encapsulate their genome during viral particle assembly. The small terminase (TerS) component of this DNA-packaging machinery acts as a molecular ...Tailed bacteriophages use a DNA-packaging motor to encapsulate their genome during viral particle assembly. The small terminase (TerS) component of this DNA-packaging machinery acts as a molecular matchmaker that recognizes both the viral genome and the main motor component, the large terminase (TerL). However, how TerS binds DNA and the TerL protein remains unclear. Here we identified gp83 of the thermophilic bacteriophage P74-26 as the TerS protein. We found that TerS oligomerizes into a nonamer that binds DNA, stimulates TerL ATPase activity, and inhibits TerL nuclease activity. A cryo-EM structure of TerS revealed that it forms a ring with a wide central pore and radially arrayed helix-turn-helix domains. The structure further showed that these helix-turn-helix domains, which are thought to bind DNA by wrapping the double helix around the ring, are rigidly held in an orientation distinct from that seen in other TerS proteins. This rigid arrangement of the putative DNA-binding domain imposed strong constraints on how TerS can bind DNA. Finally, the TerS structure lacked the conserved C-terminal β-barrel domain used by other TerS proteins for binding TerL. This suggests that a well-ordered C-terminal β-barrel domain is not required for TerS to carry out its matchmaking function. Our work highlights a thermophilic system for studying the role of small terminase proteins in viral maturation and presents the structure of TerS, revealing key differences between this thermophilic phage and its mesophilic counterparts.
External linksJ Biol Chem / PubMed:32014998 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.8 Å
Structure data

21012

6v1i

EMDB-21012: A small terminase protein from a thermophilic phage with a fixed helix-turn-helix geometry, symmetric
PDB-6v1i: Cryo-EM reconstruction of the thermophilic bacteriophage P74-26 small terminase- symmetric
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-21013:
Cryo-EM reconstruction of the thermophilic bacteriophage P74-26 small terminase, asymmetric I
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-21014:
Cryo-EM reconstruction of the thermophilic bacteriophage P74-26 small terminase- asymmetric II
Method: EM (single particle) / Resolution: 4.8 Å

Source
  • thermus virus p74-26
KeywordsVIRAL PROTEIN / small terminase / bacteriophage / helix-turn-helix / motor

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