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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Published inViruses Vol. 14; no. 10; p. 2215
Main Authors Lokareddy, Ravi K., Hou, Chun-Feng David, Li, Fenglin, Yang, Ruoyu, Cingolani, Gino
Format Journal Article
LanguageEnglish
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
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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.
AbstractList 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.
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.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.
Audience Academic
Author Cingolani, Gino
Li, Fenglin
Lokareddy, Ravi K.
Yang, Ruoyu
Hou, Chun-Feng David
AuthorAffiliation Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA
AuthorAffiliation_xml – name: Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA
Author_xml – sequence: 1
  givenname: Ravi K.
  orcidid: 0000-0002-5357-1857
  surname: Lokareddy
  fullname: Lokareddy, Ravi K.
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  orcidid: 0000-0002-1820-9588
  surname: Hou
  fullname: Hou, Chun-Feng David
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  givenname: Fenglin
  orcidid: 0000-0001-7932-0071
  surname: Li
  fullname: Li, Fenglin
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  givenname: Ruoyu
  surname: Yang
  fullname: Yang, Ruoyu
– sequence: 5
  givenname: Gino
  surname: Cingolani
  fullname: Cingolani, Gino
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Keywords X-ray crystallography
TerS
bacteriophages
herpesviruses
terminase subunits
viral genome packaging
cryo-EM
Language English
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Snippet The genome packaging motor of bacteriophages and herpesviruses is built by two terminase subunits, known as large (TerL) and small (TerS), both essential for...
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proquest
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pubmed
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StartPage 2215
SubjectTerms 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
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Title Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function
URI https://www.ncbi.nlm.nih.gov/pubmed/36298770
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https://pubmed.ncbi.nlm.nih.gov/PMC9611059
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Volume 14
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