Exclusion of small terminase mediated DNA threading models for genome packaging in bacteriophage T4
Identifieur interne : 001536 ( Ncbi/Curation ); précédent : 001535; suivant : 001537Exclusion of small terminase mediated DNA threading models for genome packaging in bacteriophage T4
Auteurs : Song Gao [États-Unis, République populaire de Chine] ; Liang Zhang [États-Unis] ; Venigalla B. Rao [États-Unis]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 2016.
Descripteurs français
- KwdFr :
- ADN viral (), ADN viral (physiologie), Assemblage viral, Bactériophage T4 (physiologie), Endodeoxyribonucleases (), Endodeoxyribonucleases (physiologie), Escherichia coli (virologie), Génome viral, Liaison aux protéines, Modèles moléculaires, Protéines de liaison à l'ADN (), Protéines de liaison à l'ADN (physiologie), Protéines virales (), Protéines virales (physiologie), Structure en hélice alpha, Structure tertiaire des protéines.
- MESH :
- physiologie : ADN viral, Bactériophage T4, Endodeoxyribonucleases, Protéines de liaison à l'ADN, Protéines virales.
- virologie : Escherichia coli.
- ADN viral, Assemblage viral, Endodeoxyribonucleases, Génome viral, Liaison aux protéines, Modèles moléculaires, Protéines de liaison à l'ADN, Protéines virales, Structure en hélice alpha, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Bacteriophage T4 (physiology), DNA, Viral (chemistry), DNA, Viral (physiology), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (physiology), Endodeoxyribonucleases (chemistry), Endodeoxyribonucleases (physiology), Escherichia coli (virology), Genome, Viral, Models, Molecular, Protein Binding, Protein Conformation, alpha-Helical, Protein Structure, Tertiary, Viral Proteins (chemistry), Viral Proteins (physiology), Virus Assembly.
- MESH :
- chemical , chemistry : DNA, Viral, DNA-Binding Proteins, Endodeoxyribonucleases, Viral Proteins.
- physiology : Bacteriophage T4, DNA, Viral, DNA-Binding Proteins, Endodeoxyribonucleases, Viral Proteins.
- virology : Escherichia coli.
- Genome, Viral, Models, Molecular, Protein Binding, Protein Conformation, alpha-Helical, Protein Structure, Tertiary, Virus Assembly.
Abstract
Tailed bacteriophages and herpes viruses use powerful molecular machines to package their genomes. The packaging machine consists of three components: portal, motor (large terminase; TerL) and regulator (small terminase; TerS). Portal, a dodecamer, and motor, a pentamer, form two concentric rings at the special five-fold vertex of the icosahedral capsid. Powered by ATPase, the motor ratchets DNA into the capsid through the portal channel. TerS is essential for packaging, particularly for genome recognition, but its mechanism is unknown and controversial. Structures of gear-shaped TerS rings inspired models that invoke DNA threading through the central channel. Here, we report that mutations of basic residues that line phage T4 TerS (gp16) channel do not disrupt DNA binding. Even deletion of the entire channel helix retained DNA binding and produced progeny phage
Url:
DOI: 10.1093/nar/gkw184
PubMed: 26984529
PubMed Central: 4872099
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PMC:4872099Le document en format XML
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<term>DNA, Viral (physiology)</term>
<term>DNA-Binding Proteins (chemistry)</term>
<term>DNA-Binding Proteins (physiology)</term>
<term>Endodeoxyribonucleases (chemistry)</term>
<term>Endodeoxyribonucleases (physiology)</term>
<term>Escherichia coli (virology)</term>
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<term>Protein Binding</term>
<term>Protein Conformation, alpha-Helical</term>
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<term>Viral Proteins (physiology)</term>
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<front><div type="abstract" xml:lang="en"><p>Tailed bacteriophages and herpes viruses use powerful molecular machines to package their genomes. The packaging machine consists of three components: portal, motor (large terminase; TerL) and regulator (small terminase; TerS). Portal, a dodecamer, and motor, a pentamer, form two concentric rings at the special five-fold vertex of the icosahedral capsid. Powered by ATPase, the motor ratchets DNA into the capsid through the portal channel. TerS is essential for packaging, particularly for genome recognition, but its mechanism is unknown and controversial. Structures of gear-shaped TerS rings inspired models that invoke DNA threading through the central channel. Here, we report that mutations of basic residues that line phage T4 TerS (gp16) channel do not disrupt DNA binding. Even deletion of the entire channel helix retained DNA binding and produced progeny phage <italic>in vivo</italic>
. On the other hand, large oligomers of TerS (11-mers/12-mers), but not small oligomers (trimers to hexamers), bind DNA. These results suggest that TerS oligomerization creates a large outer surface, which, but not the interior of the channel, is critical for function, probably to wrap viral genome around the ring during packaging initiation. Hence, models involving TerS-mediated DNA threading may be excluded as an essential mechanism for viral genome packaging.</p>
</div>
</front>
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