Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 3, Pages 2092-2102Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.407460
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Funding
- National Institutes of Health [R01AI41599, GM037705]
- National Institutes of Health
- National Science Foundation
- Ministerio de Ciencia e Innovacion of Spain [BFU2010-16382, FIS2010-10552-E]
- Juan de la Cierva from the Ministerio de Ciencia e Innovacion of Spain
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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 x 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.
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