Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-10-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/14/10/2215 |
| _version_ | 1797469659093532672 |
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| author | Ravi K. Lokareddy Chun-Feng David Hou Fenglin Li Ruoyu Yang Gino Cingolani |
| author_facet | Ravi K. Lokareddy Chun-Feng David Hou Fenglin Li Ruoyu Yang Gino Cingolani |
| author_sort | Ravi K. Lokareddy |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-09T19:23:20Z |
| format | Article |
| id | doaj.art-cf6c82daec884b2aaf9a6a07bb019d97 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-09T19:23:20Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-cf6c82daec884b2aaf9a6a07bb019d972023-11-24T03:09:31ZengMDPI AGViruses1999-49152022-10-011410221510.3390/v14102215Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological FunctionRavi K. Lokareddy0Chun-Feng David Hou1Fenglin Li2Ruoyu Yang3Gino Cingolani4Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USADepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USADepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USADepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USADepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USAThe 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.https://www.mdpi.com/1999-4915/14/10/2215viral genome packagingterminase subunitsTerScryo-EMX-ray crystallographybacteriophages |
| spellingShingle | Ravi K. Lokareddy Chun-Feng David Hou Fenglin Li Ruoyu Yang Gino Cingolani Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function Viruses viral genome packaging terminase subunits TerS cryo-EM X-ray crystallography bacteriophages |
| title | Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function |
| title_full | Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function |
| title_fullStr | Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function |
| title_full_unstemmed | Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function |
| title_short | Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function |
| title_sort | viral small terminase a divergent structural framework for a conserved biological function |
| topic | viral genome packaging terminase subunits TerS cryo-EM X-ray crystallography bacteriophages |
| url | https://www.mdpi.com/1999-4915/14/10/2215 |
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