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Structure-based assembly of protein complexes in yeast

Item Type:Article
Title:Structure-based assembly of protein complexes in yeast
Creators Name:Aloy, P. and Boettcher, B. and Ceulemans, H. and Leutwein, C. and Mellwig, C. and Fischer, S. and Gavin, A.C. and Bork, P. and Superti-Furga, G. and Serrano, L. and Russell, R.B.
Abstract:Images of entire cells are preceding atomic structures of the separate molecular machines that they contain. The resulting gap in knowledge can be partly bridged by protein-protein interactions, bioinformatics, and electron microscopy. Here we use interactions of known three-dimensional structure to model a large set of yeast complexes, which we also screen by electron microscopy. For 54 of 102 complexes, we obtain at least partial models of interacting subunits. For 29, including the exosome, the chaperonin containing TCP-1, a 3'-messenger RNA degradation complex, and RNA polymerase II, the process suggests atomic details not easily seen by homology, involving the combination of two or more known structures. We also consider interactions between complexes (cross-talk) and use these to construct a structure-based network of molecular machines in the cell.
Keywords:Chaperonins, Computational Biology, Computer-Assisted Image Processing, Electron Microscopy, Biological Models, Molecular Models, Nuclear Proteins, Protein Binding, Protein Conformation, Protein Interaction Mapping, Tertiary Protein Structure, RNA Polymerase II, Ribonuclease P, Saccharomyces Cerevisiae, Saccharomyces Cerevisiae Proteins, Transcription Factors
Publisher:American Association for the Advancement of Science
Page Range:2026-2029
Date:26 March 2004
Official Publication:https://doi.org/10.1126/science.1092645
PubMed:View item in PubMed

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