Please use this identifier to cite or link to this item:
|Title:||Overproduction, purification, and characterization of DNA-binding protein P19 of bacteriophage PRD1|
|Authors:||Pakula, Tiina M.; Caldentey, Javier; Gutiérrez Armenta, Crisanto; Olkkonen, Vesa M.; Bamford, Dennis H.; Salas, Margarita|
|Keywords:||Protection of single-stranded DNA against nuclease P1|
Phage λ pL promoter
|Citation:||Gene 126(1): 99-104 (1993)|
|Abstract:||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.|
|Publisher version (URL):||http://dx.doi.org/10.1016/0378-1119(93)90595-T|
|Appears in Collections:||(CBM) Artículos|
Files in This Item:
There are no files associated with this item.
Show full item record
WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.