| Autor: |
Mangel WF; Department of Biology, Brookhaven National Laboratory, 50 Bell Avenue, Upton, New York 11973, USA., McGrath WJ; Department of Biology, Brookhaven National Laboratory, 50 Bell Avenue, Upton, New York 11973, USA., Xiong K; Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.; Broad Institute of MIT and Harvard, Cambridge, Massachusetts 02142, USA., Graziano V; Department of Biology, Brookhaven National Laboratory, 50 Bell Avenue, Upton, New York 11973, USA., Blainey PC; Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.; Broad Institute of MIT and Harvard, Cambridge, Massachusetts 02142, USA. |
| Abstrakt: |
Recently, we showed the adenovirus proteinase interacts productively with its protein substrates in vitro and in vivo in nascent virus particles via one-dimensional diffusion along the viral DNA. The mechanism by which this occurs has heretofore been unknown. We show sliding of these proteins along DNA occurs on a new vehicle in molecular biology, a 'molecular sled' named pVIc. This 11-amino acid viral peptide binds to DNA independent of sequence. pVIc slides on DNA, exhibiting the fastest one-dimensional diffusion constant, 26±1.8 × 10(6) (bp)(2) s(-1). pVIc is a 'molecular sled,' because it can slide heterologous cargos along DNA, for example, a streptavidin tetramer. Similar peptides, for example, from the C terminus of β-actin or NLSIII of the p53 protein, slide along DNA. Characteristics of the 'molecular sled' in its milieu (virion, nucleus) have implications for how proteins in the nucleus of cells interact and imply a new form of biochemistry, one-dimensional biochemistry. |
