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Título: | Intrinsic disorder of the bacterial cell division protein ZipA: Coil-to-brush conformational transition |
Autor: | López-Montero, Iván; López-Navajas, Pilar CSIC ; Mingorance, Jesús CSIC ORCID; Rivas, Germán CSIC ORCID CVN ; Vélez, Marisela CSIC ORCID; Vicente, Miguel CSIC ORCID; Monroy, Francisco | Palabras clave: | Polymer theory E. coli Langmuir monolayers |
Fecha de publicación: | ago-2013 | Editor: | Federation of American Societies for Experimental Biology | Citación: | FASEB Journal 27(8): 3363-3375 (2013) | Resumen: | The full-length ZipA protein from Escherichia coli, one of the essential elements of the cell division machinery, was studied in a surface model built as adsorbed monolayers. The interplay between lateral packing and molecular conformation was probed using a combined methodology based on the scaling analysis of the surface pressure isotherms and ellipsometry measurements of the monolayer thickness. The observed behavior is compatible with the one expected for an intrinsically disordered and highly flexible protein that is preferentially structured in a random coil conformation. At low grafting densities, ZipA coils organize in a mushroom-like regime, whereas a coil-to-brush transition occurs on increasing lateral packing. The structural results suggest a functional scenario in which ZipA acts as a flexible tether anchoring bacterial proto-ring elements to the membrane during the earlier stages of division. | Versión del editor: | https://doi.org/10.1096/fj.12-224337 | URI: | http://hdl.handle.net/10261/182609 | DOI: | 10.1096/fj.12-224337 | ISSN: | 0892-6638 | E-ISSN: | 1530-6860 |
Aparece en las colecciones: | (ICP) Artículos (CIB) Artículos (CNB) Artículos |
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