Document Detail


Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: II. adenovirus proteinase is activated in an unusual one-dimensional biochemical reaction.
MedLine Citation:
PMID:  23043137     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Late in an adenovirus infection, the viral proteinase (AVP) becomes activated to process virion precursor proteins used in virus assembly. AVP is activated by two cofactors, the viral DNA and pVIc, an 11-amino acid peptide originating from the C terminus of the precursor protein pVI. There is a conundrum in the activation of AVP in that AVP and pVI are sequence-independent DNA-binding proteins with nm equilibrium dissociation constants such that in the virus particle, they are predicted to be essentially irreversibly bound to the viral DNA. Here, we resolve that conundrum by showing that activation of AVP takes place on the one-dimensional contour of DNA. In vitro, pVI, a substrate, slides on DNA via one-dimensional diffusion, D(1) = 1.45 × 10(6) bp(2)/s, until it binds to AVP also on the same DNA molecule. AVP, partially activated by being bound to DNA, excises pVIc, which binds to the AVP molecule that cut it out. pVIc then forms a disulfide bond with AVP forming the fully active AVP-pVIc complex bound to DNA. In vivo, in heat-disrupted immature virus, AVP was also activated by pVI in DNA-dependent reactions. This activation mechanism illustrates a new paradigm for virion maturation and a new way, by sliding on DNA, for bimolecular complexes to form among proteins not involved in DNA metabolism.
Authors:
Vito Graziano; Guobin Luo; Paul C Blainey; Ana J Pérez-Berná; William J McGrath; S Jane Flint; Carmen San Martín; X Sunney Xie; Walter F Mangel
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-10-07
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-21     Completed Date:  2013-03-26     Revised Date:  2014-01-24    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2068-80     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenoviruses, Human / enzymology*,  genetics
Amino Acid Sequence
Capsid Proteins / chemistry,  genetics,  metabolism*
Cysteine Endopeptidases / chemistry,  genetics,  metabolism*
DNA, Viral / chemistry,  metabolism*
Disulfides / chemistry,  metabolism
Enzyme Activation
Humans
Kinetics
Molecular Sequence Data
Protein Binding
Protein Precursors / chemistry,  genetics,  metabolism*
Recombinant Proteins / chemistry,  genetics,  metabolism
Thermodynamics
Virion / enzymology*,  genetics
Grant Support
ID/Acronym/Agency:
DP1 OD000277/OD/NIH HHS; GM037705/GM/NIGMS NIH HHS; R01AI41599/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Capsid Proteins; 0/DNA, Viral; 0/Disulfides; 0/Protein Precursors; 0/Recombinant Proteins; 0/polypeptide VI, adenovirus; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.39/adenain
Comments/Corrections

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