title: Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: IV. viral proteinase slides along DNA to locate and process its substrates.
abstract: Precursor proteins used in the assembly of adenovirus virions must be processed by the virally encoded adenovirus proteinase (AVP) before the virus particle becomes infectious. An activated adenovirus proteinase, the AVP-pVIc complex, was shown to slide along viral DNA with an extremely fast one-dimensional diffusion constant, 21.0 ± 1.9 × 10(6) bp(2)/s. In principle, one-dimensional diffusion can provide a means for DNA-bound proteinases to locate and process DNA-bound substrates. Here, we show that this is correct. In vitro, AVP-pVIc complexes processed a purified virion precursor protein in a DNA-dependent reaction; in a quasi in vivo environment, heat-disrupted ts-1 virions, AVP-pVIc complexes processed five different precursor proteins in DNA-dependent reactions. Sliding of AVP-pVIc complexes along DNA illustrates a new biochemical mechanism by which a proteinase can locate its substrates, represents a new paradigm for virion maturation, and reveals a new way of exploiting the surface of DNA.
authors.affiliation: Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
authors.forename: Paul C
authors.initials: PC
authors.lastname: Blainey
authors.forename: Vito
authors.initials: V
authors.lastname: Graziano
authors.forename: Ana J
authors.initials: AJ
authors.lastname: Pérez-Berná
authors.forename: William J
authors.initials: WJ
authors.lastname: McGrath
authors.forename: S Jane
authors.initials: SJ
authors.lastname: Flint
authors.forename: Carmen
authors.initials: C
authors.lastname: San Martín
authors.forename: X Sunney
authors.initials: XS
authors.lastname: Xie
authors.forename: Walter F
authors.initials: WF
authors.lastname: Mangel
mesh_terms: D000260:Adenoviruses, Human / Q000201:enzymology* / Q000235:genetics; D000595:Amino Acid Sequence; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004279:DNA, Viral / Q000737:chemistry* / Q000378:metabolism; D004789:Enzyme Activation; D004926:Escherichia coli / Q000235:genetics; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011498:Protein Precursors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics; D014771:Virion / Q000201:enzymology* / Q000235:genetics
chemical_list: D036022:Capsid Proteins; D004279:DNA, Viral; D011498:Protein Precursors; D011994:Recombinant Proteins; C090876:polypeptide VI, adenovirus; D003546:Cysteine Endopeptidases; C091827:adenain