Cancer Institute A national cancer institute
designated cancer center

Stephen Quake

Publication Details

  • Proteome-wide protein interaction measurements of bacterial proteins of unknown function PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Meier, M., Sit, R. V., Quake, S. R. 2013; 110 (2): 477-482


    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.

    View details for DOI 10.1073/pnas.1210634110

    View details for Web of Science ID 000313906600027

    View details for PubMedID 23267104

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