Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/130726
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | The bacteriocin AS-48 requires dimer dissociation followed by hydrophobic interactions with the membrane for antibacterial activity |
Autor: | Cebrián, R.; Martínez-Bueno, M.; Valdivia, E.; Albert, Armando CSIC ORCID; Maqueda, M.; Sánchez-Barrena, María José CSIC ORCID | Fecha de publicación: | 2015 | Editor: | Academic Press | Citación: | Journal of Structural Biology 190: 162- 172 (2015) | Resumen: | © 2015 Elsevier Inc. The molecular mechanism underlining the antibacterial activity of the bacteriocin AS-48 is not known, and two different and opposite alternatives have been proposed. Available data suggested that the interaction of positively charged amino acids of AS-48 with the membrane would produce membrane destabilization and disruption. Alternatively, it has been proposed that AS-48 activity could rely on the effective insertion of the bacteriocin into the membrane. The biological and structural properties of the AS-48<inf>G13K/L40K</inf> double mutant were investigated to shed light on this subject. Compared with the wild type, the mutant protein suffered an important reduction in the antibacterial activity. Biochemical and structural studies of AS-48<inf>G13K/L40K</inf> mutant suggest the basis of its decreased antimicrobial activity. Lipid cosedimentation assays showed that the membrane affinity of AS-48<inf>G13K/L40K</inf> is 12-fold lower than that observed for the wild type. L40K mutation is responsible for this reduced membrane affinity and thus, hydrophobic interactions are involved in membrane association. Furthermore, the high-resolution crystal structure of AS-48<inf>G13K/L40K</inf>, together with the study of its dimeric character in solution showed that G13K stabilizes the inactive water-soluble dimer, which displays a reduced dipole moment. Our data suggest that the cumulative effect of these three affected properties reduces AS-48 activity, and point out that the bactericidal effect is achieved by the electrostatically driven approach of the inactive water-soluble dimer towards the membrane, followed by the dissociation and insertion of the protein into the lipid bilayer. | URI: | http://hdl.handle.net/10261/130726 | DOI: | 10.1016/j.jsb.2015.03.006 | Identificadores: | doi: 10.1016/j.jsb.2015.03.006 issn: 1095-8657 |
Aparece en las colecciones: | (IQF) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
39
checked on 20-abr-2024
WEB OF SCIENCETM
Citations
37
checked on 28-feb-2024
Page view(s)
213
checked on 24-abr-2024
Download(s)
93
checked on 24-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.