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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 CSIC ORCID; Olkkonen, Vesa M.; Bamford, Dennis H.; Salas, Margarita CSIC ORCID | Palabras clave: | Protection of single-stranded DNA against nuclease P1 Phage λ pL promoter Protein purification Gel-shift assay |
Fecha de publicación: | 15-abr-1993 | Editor: | Elsevier | Citación: | Gene 126(1): 99-104 (1993) | 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 | DOI: | 10.1016/0378-1119(93)90595-T | ISSN: | 0378-1119 |
Aparece en las colecciones: | (CBM) Artículos |
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