Document Type
Article
Publication Date
10-8-2022
Abstract
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.
Recommended Citation
Lokareddy, Ravi K.; Hou, Chun-Feng David; Li, Fenglin; Yang, Ruoyu; and Cingolani, Gino, "Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function." (2022). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 227.
https://jdc.jefferson.edu/bmpfp/227
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
PubMed ID
36298770
Language
English
Comments
This is the author's final published version in Viruses, Volume 14, Issue 10, October 2022, Article number 2215.
The published version is available online at https://doi.org/10.3390/v14102215. Copyright © 2022 by the authors. Licensee MDPI, Basel, Switzerland.