Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12857/116343
Title: Transient Interactions of a Cytosolic Protein with Macromolecular and Vesicular Cosolutes: Unspecific and Specific Effects
Authors: Ceccon, Alberto 
Busato, Mirko 
Pérez Santero, Silvia
D'Onofrio, Mariapina 
Musiani, Francesco
Giorgetti, Alejandro 
Assfalg, Michael 
Keywords: NMR spectroscopy;data-driven docking;intracellular environment;macromolecular crowding;protein-protein interactions
Keywords Plus: ACID-BINDING-PROTEIN;COARSE-GRAINED MODEL;MOLECULAR-DYNAMICS;LIGAND-BINDING;NMR;FLUORESCENCE;RELAXATION;COMPLEX;DOMAIN;WEAK
Mesh headings: Hydroxysteroid Dehydrogenases;Macromolecular Substances
Secondary Mesh headings: Binding Sites;Cytosol;Humans;Lipid Bilayers;Molecular Dynamics Simulation;Muramidase;Nuclear Magnetic Resonance, Biomolecular;Protein Interaction Domains and Motifs;Spectrometry, Fluorescence;Ubiquitin
Issue Date: Dec-2015
Publisher: WILEY-V C H VERLAG GMBH
Journal: Chembiochem : a European journal of chemical biology 
Abstract: 
Cytosolic proteins do not occur as isolated but are exposed to many interactions within a crowded cellular environment. We investigated the associations between a test cytosolic protein, human ileal bile acid binding protein (IBABP), and model cosolutes mimicking macromolecular and lipid membrane intracellular components. Using fluorescence spectroscopy, heteronuclear NMR, and molecular dynamics, we found that IBABP associated weakly with anionic lipid vesicles and experienced transient unspecific contacts with albumin. Localized dynamic perturbations were observed even in the case of apparent unspecific binding. IBABP and ubiquitin did not display mutually attractive forces, whereas IBABP associated specifically with lysozyme. A structural model of the IBABP-lysozyme complex was obtained by data-driven docking simulation. Presumably, all the interactions shown here contribute to modulating functional communication of a protein in its native environment.
URI: http://hdl.handle.net/20.500.12857/116343
ISSN: 14394227
DOI: 10.1002/cbic.201500451
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