Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/38946
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Oligomeric Structures of the Phage Ø29 Histone-like Protein p6 |
Autor: | Abril, Ana M.; Marco, Sergio; Carrascosa, José L. CSIC ORCID; Salas, Margarita CSIC ORCID ; Hermoso, José Miguel | Palabras clave: | Bacteriophage Ø29 Histone-like protein Oligomers Electron microscopy |
Fecha de publicación: | 24-sep-1999 | Editor: | Elsevier | Citación: | Journal of Molecular Biology 292(3): 581-588 (1999) | 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 | DOI: | 10.1006/jmbi.1999.3078 | ISSN: | 0022-2836 |
Aparece en las colecciones: | (CBM) Artículos (CNB) Artículos |
Mostrar el registro completo
CORE Recommender
SCOPUSTM
Citations
11
checked on 10-abr-2024
WEB OF SCIENCETM
Citations
11
checked on 26-feb-2024
Page view(s)
339
checked on 17-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.