title: Proteome-wide protein interaction measurements of bacterial proteins of unknown function.
abstract: Despite the enormous proliferation of bacterial genome data, surprisingly persistent collections of bacterial proteins have resisted functional annotation. In a typical genome, roughly 30% of genes have no assigned function. Many of these proteins are conserved across a large number of bacterial genomes. To assign a putative function to these conserved proteins of unknown function, we created a physical interaction map by measuring biophysical interaction of these proteins. Binary protein--protein interactions in the model organism Streptococcus pneumoniae (TIGR4) are measured with a microfluidic high-throughput assay technology. In some cases, informatic analysis was used to restrict the space of potential binding partners. In other cases, we performed in vitro proteome-wide interaction screens. We were able to assign putative functions to 50 conserved proteins of unknown function that we studied with this approach.
authors.affiliation: Department of Applied Physics and Bioengineering, Stanford University, Stanford, CA 94305, USA.
authors.forename: Matthias
authors.initials: M
authors.lastname: Meier
authors.forename: Rene V
authors.initials: RV
authors.lastname: Sit
authors.forename: Stephen R
authors.initials: SR
authors.lastname: Quake
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D057166:High-Throughput Screening Assays; D046210:Microfluidic Analytical Techniques; D058977:Molecular Sequence Annotation / Q000379:methods*; D025941:Protein Interaction Mapping / Q000379:methods*; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D013296:Streptococcus pneumoniae / Q000235:genetics*
chemical_list: D001426:Bacterial Proteins; D020543:Proteome