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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.

Author(s): Graziano, Vito; Luo, Guobin; Blainey, Paul C.; Pérez-Berná, Ana J.; McGrath, William J.; et al

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dc.contributor.authorGraziano, Vito-
dc.contributor.authorLuo, Guobin-
dc.contributor.authorBlainey, Paul C.-
dc.contributor.authorPérez-Berná, Ana J.-
dc.contributor.authorMcGrath, William J.-
dc.contributor.authorFlint, S. Jane-
dc.contributor.authorSan Martín, Carmen-
dc.contributor.authorXie, X. Sunney-
dc.contributor.authorMangel, Walter F.-
dc.date.accessioned2020-02-27T22:16:40Z-
dc.date.available2020-02-27T22:16:40Z-
dc.date.issued2013-01en_US
dc.identifier.citationGraziano, Vito, Luo, Guobin, Blainey, Paul C, Pérez-Berná, Ana J, McGrath, William J, Flint, S Jane, San Martín, Carmen, Xie, X Sunney, Mangel, Walter F. (2013). 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.. The Journal of Biological Chemistry, 288 (3), 2068 - 2080. doi:10.1074/jbc.M112.407312en_US
dc.identifier.issn0021-9258-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1rz0x-
dc.description.abstractLate 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.en_US
dc.format.extent2068 - 2080en_US
dc.languageengen_US
dc.language.isoen_USen_US
dc.relation.ispartofThe Journal of Biological Chemistryen_US
dc.rightsFinal published version. Article is made available in OAR by the publisher's permission or policy.en_US
dc.titleRegulation 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.en_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1074/jbc.M112.407312-
dc.identifier.eissn1083-351X-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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