Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function

• Published in: Viruses Vol. 14; no. 10; p. 2215
• Main Authors: Lokareddy, Ravi K., Hou, Chun-Feng David, Li, Fenglin, Yang, Ruoyu, Cingolani, Gino
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.10.2022; MDPI
• Subjects: Adenosine Triphosphate; Amino acids; bacteriophages; Bacteriophages - chemistry; Bacteriophages - genetics; Conserved sequence; cryo-EM; Cryoelectron Microscopy; DNA Packaging; DNA, Viral - chemistry; E coli; Electron microscopy; Endodeoxyribonucleases - genetics; Environmental conditions; Genomes; Herpes viruses; Mechanical properties; Phages; Phylogenetics; Physiological aspects; Protein structure; Proteins; Quaternary structure; Review; Salmonella; Structure; Symmetry; Terminase; terminase subunits; TerS; viral genome packaging; Viral proteins; Viral Proteins - genetics; Virus Assembly - genetics; Virus research; X-ray crystallography; United States; X-ray crystallography; TerS; bacteriophages; herpesviruses; terminase subunits; viral genome packaging; cryo-EM
• ISSN: 1999-4915; 1999-4915
• DOI: 10.3390/v14102215

The genome packaging motor of bacteriophages and herpesviruses is built by two terminase subunits, known as large (TerL) and small (TerS), both essential for viral genome packaging. TerL structure, composition, and assembly to an empty capsid, as well as the mechanisms of ATP-dependent DNA packaging, have been studied in depth, shedding light on the chemo-mechanical coupling between ATP hydrolysis and DNA translocation. Instead, significantly less is known about the small terminase subunit, TerS, which is dispensable or even inhibitory in vitro, but essential in vivo. By taking advantage of the recent revolution in cryo-electron microscopy (cryo-EM) and building upon a wealth of crystallographic structures of phage TerSs, in this review, we take an inventory of known TerSs studied to date. Our analysis suggests that TerS evolved and diversified into a flexible molecular framework that can conserve biological function with minimal sequence and quaternary structure conservation to fit different packaging strategies and environmental conditions.