Document Detail


The enzymology of a viral genome packaging motor is influenced by the assembly state of the motor subunits.
MedLine Citation:
PMID:  23134123     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Terminase enzymes are responsible for the excision of a single genome from a concatemeric precursor (genome maturation) and concomitant packaging of DNA into the capsid shell. Here, we demonstrate that lambda terminase can be purified as a homogeneous "protomer" species, and we present a kinetic analysis of the genome maturation and packaging activities of the protomeric enzyme. The protomer assembles into a distinct maturation complex at the cos sequence of a concatemer. This complex rapidly nicks the duplex to form the mature left end of the viral genome, which is followed by procapsid binding, activation of the packaging ATPase, and translocation of the duplex into the capsid interior by the terminase motor complex. Genome packaging by the protomer shows high fidelity with only the mature left end of the duplex inserted into the capsid shell. In sum, the data show that the terminase protomer exhibits catalytic activity commensurate with that expected of a bone fide genome maturation and packaging complex in vivo and that both catalytically competent complexes are composed of four terminase protomers assembled into a ringlike structure that encircles duplex DNA. This work provides mechanistic insight into the coordinated catalytic activities of terminase enzymes in virus assembly that can be generalized to all of the double-stranded DNA viruses.
Authors:
Benjamin T Andrews; Carlos Enrique Catalano
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-11-07
Journal Detail:
Title:  Biochemistry     Volume:  51     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-20     Completed Date:  2013-01-22     Revised Date:  2013-12-04    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  9342-53     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
DNA Packaging
Endodeoxyribonucleases / metabolism*
Genome, Viral*
Hydrolysis
Kinetics
Promoter Regions, Genetic
Grant Support
ID/Acronym/Agency:
F32 GM090565/GM/NIGMS NIH HHS; F32GM-905652/GM/NIGMS NIH HHS; GM088186/GM/NIGMS NIH HHS; R01 GM088186/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
8L70Q75FXE/Adenosine Triphosphate; EC 3.1.-/Endodeoxyribonucleases; EC 3.1.-/terminase
Comments/Corrections

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