Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/39360
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Título : Overproduction, purification, and characterization of DNA-binding protein P19 of bacteriophage PRD1
Autor : Pakula, Tiina M., Caldentey, Javier, Gutiérrez Armenta, Crisanto, Olkkonen, Vesa M., Bamford, Dennis H., Salas, Margarita
Palabras clave : Protection of single-stranded DNA against nuclease P1
Phage λ pL promoter
Protein purification
Gel-shift assay
Fecha de publicación : 15-Apr-1993
Editor: Elsevier
Resumen: The early protein, P 19, of bacteriophage PRD1 was purified after overexpression of the cloned gene, XIX, in Escherichia coli DH5α cells. The purified protein binds as multimers to single-stranded DNA (ssDNA), and with a lower affinity to double-stranded DNA (dsDNA), without sequence-specificity. Two distinct P19-ssDNA complexes were discovered in gel- mobility-shift assays at different protein:DNA ratios. P 19 was capable of fully protecting ssDNA against nuclease P1. Electron microscopy of protein P19-ssDNA complexes showed DNA molecules which were extensively coated with protein and whose contour length was clearly reduced by P 19 binding. The results suggest that P 19 binds to ssDNA with moderate cooperativity and are consistent with the DNA being wrapped around the P 19 multimers.
Versión del editor: http://dx.doi.org/10.1016/0378-1119(93)90595-T
URI : http://hdl.handle.net/10261/39360
ISSN: 0378-1119
DOI: 10.1016/0378-1119(93)90595-T
Citación : Gene 126(1): 99-104 (1993)
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