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The small terminase subunit (TerS) is crucial for viral genome packaging, despite being dispensable in vitro. This review explores TerS evolution, revealing a flexible framework adapting to diverse viral strategies.

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Bacteriophage and herpesvirus genome packaging relies on terminase complexes, comprising large (TerL) and small (TerS) subunits.
  • TerL's role in DNA packaging and ATP-dependent translocation is well-understood, but TerS function remains enigmatic.
  • TerS is essential in vivo for viral packaging, yet often dispensable or inhibitory in in vitro experimental settings.

Purpose of the Study:

  • To review and inventory known small terminase (TerS) structures and functions across various viruses.
  • To elucidate the evolutionary diversification of TerS and its impact on viral genome packaging strategies.

Main Methods:

  • Compilation and analysis of existing crystallographic structures of phage TerS proteins.
  • Leveraging advancements in cryo-electron microscopy (cryo-EM) for structural insights.
  • Comparative analysis of TerS sequences and quaternary structures.

Main Results:

  • TerS exhibits significant sequence and structural diversity across different viral families.
  • Despite variations, TerS subunits appear to function as flexible molecular frameworks.
  • Minimal conservation in sequence and quaternary structure suggests adaptation to specific packaging mechanisms and conditions.

Conclusions:

  • The small terminase (TerS) subunit has evolved a flexible framework, allowing functional conservation despite structural diversification.
  • Understanding TerS evolution provides insights into the adaptability of viral genome packaging machinery.
  • Further structural and functional studies of TerS are needed to fully comprehend its role in viral replication.