Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/38946
Share/Impact:
Título : Oligomeric Structures of the Phage Ø29 Histone-like Protein p6
Autor : Abril, Ana M., Marco, Sergio, Carrascosa, José L., Salas, Margarita, Hermoso, José Miguel
Palabras clave : Bacteriophage Ø29
Histone-like protein
Oligomers
Electron microscopy
Fecha de publicación : 24-Sep-1999
Editor: Elsevier
Resumen: Protein p6 of Bacillus subtilis phage Ø29 has been described as a histone-like protein, playing a role in genome organization and compaction, on the basis of its high intracellular abundance, its pleiotropic effect, and its ability to bind and highly compact the whole Ø29 DNA in vitro. Protein p6 forms large multimeric nucleoprotein complexes in which a right-handed superhelical DNA wraps toroidally around the protein core. Analytical ultracentrifugation analysis, at the concentration estimated in vivo (at least 1 mM), showed that protein p6 self-associates into elongated oligomers, suggesting that, in the absence of DNA, the protein could form a scaffold for DNA binding. In this work we have studied the structure of these oligomers by transmission electron microscopy and image processing. The results show that protein p6 aggregates into crooked-shaped oligomers, compatible with a helical structure. The oligomers could interact head-to-tail to form doughnut-shaped structures or they could grow into right-handed double-helical filaments by a nucleation-dependent polymerization process. The dimensions of the crooked-shaped structures are in agreement with that of the DNA in the nucleoprotein complex previously described. We propose that the crooked-shaped structures could act as a scaffold imposing the right-handed path followed by the DNA, and thus it could be considered a non-transient DNA chaperone.
Versión del editor: http://dx.doi.org/10.1006/jmbi.1999.3078
URI : http://hdl.handle.net/10261/38946
ISSN: 0022-2836
DOI: 10.1006/jmbi.1999.3078
Citación : Journal of Molecular Biology 292(3): 581-588 (1999)
Appears in Collections:(CBM) Artículos
(CNB) Artículos

Files in This Item:
There are no files associated with this item.
Show full item record
 
CSIC SFX LinksSFX Query


Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.