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J Biol Chem DOI:10.1074/jbc.M112.407460

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.

Publication TypeJournal Article
Year of Publication2013
AuthorsBlainey, PC, Graziano, V, Pérez-Berná, AJ, McGrath, WJ, S Flint, J, San Martín, C, X Xie, S, Mangel, WF
JournalJ Biol Chem
Date Published2013 Jan 18
KeywordsAdenoviruses, Human, Amino Acid Sequence, Capsid Proteins, Cysteine Endopeptidases, DNA, Viral, Enzyme Activation, Escherichia coli, Hot Temperature, Humans, Kinetics, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Precursors, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Thermodynamics, Virion

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.


Alternate JournalJ. Biol. Chem.
PubMed ID23043138
PubMed Central IDPMC3548515
Grant ListR01AI41599 / AI / NIAID NIH HHS / United States
R01 AI041599 / AI / NIAID NIH HHS / United States
R21 AI113565 / AI / NIAID NIH HHS / United States
GM037705 / GM / NIGMS NIH HHS / United States
DP1 OD000277 / OD / NIH HHS / United States
R01 GM037705 / GM / NIGMS NIH HHS / United States