Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Describing, understanding, and modulating the function of the cell require elucidation of the structures of macromolecular assemblies. Here, we describe an integrative method for modeling heteromeric complexes using as a starting point disassembly pathways determined by native mass spectrometry (MS). In this method, the pathway data and other available information are encoded as a scoring function on the positions of the subunits of the complex. The method was assessed on its ability to reproduce the native contacts in five benchmark cases with simulated MS data and two cases with real MS data. To illustrate the power of our method, we purified the yeast initiation factor 3 (eIF3) complex and characterized it by native MS and chemical crosslinking MS. We established substoichiometric binding of eIF5 and derived a model for the five-subunit eIF3 complex, at domain level, consistent with its role as a scaffold for other initiation factors.

Original publication

DOI

10.1016/j.chembiol.2014.11.010

Type

Journal article

Journal

Chem Biol

Publication Date

22/01/2015

Volume

22

Pages

117 - 128

Keywords

Eukaryotic Initiation Factor-3, Models, Molecular, Peptide Initiation Factors, Protein Binding, ROC Curve, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Tandem Mass Spectrometry