Please use this identifier to cite or link to this item:
|Título :||A new protein domain for binding to DNA through the minor groove|
|Autor :||Freire, Raimundo, Salas, Margarita, Hermoso, José Miguel|
|Palabras clave :||DNA minor groove binding|
|Fecha de publicación :||15-Sep-1994|
|Editor:||Nature Publishing Group|
|Citación :||Embo Journal 13(18):4353-360 (1994)|
|Resumen:||Protein p6 of the Bacillus subtilis phage phi 29 binds with low sequence specificity to DNA through the minor groove, forming a multimeric nucleoprotein complex that activates the initiation of phi 29 DNA replication. Deletion analysis suggested that the N-terminal part of protein p6, predicted to form an amphipathic alpha-helix, is involved in DNA binding. We have constructed site-directed mutants at the polar side of the putative alpha-helix. DNA binding and activation of initiation of phi 29 DNA replication were impaired in most of the mutant proteins obtained. A 19 amino acid peptide comprising the N-terminus of protein p6 interacted with a DNA fragment containing high-affinity signals for protein p6 binding with approximately 50-fold higher affinity than the peptide corresponding to an inactive mutant. Both wild-type peptide and protein p6 recognized the same sequences in this DNA fragment. This result, together with distamycin competition experiments, suggested that the wild-type peptide also binds to DNA through the minor groove. In addition, CD spectra of the wild-type peptide showed an increase in the alpha-helical content when bound to DNA. All these results indicate that an alpha-helical structure located in the N-terminal region of protein p6 is involved in DNA binding through the minor groove.|
|Versión del editor:||http://www.ncbi.nlm.nih.gov/pmc/articles/pmid/7925279/?tool=pubmed|
|Appears in Collections:||(CBM) Artículos|
Files in This Item:
There are no files associated with this item.
Show full item recordCSIC SFX Links
Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.