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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.

SUBMITTER: Meier M 

PROVIDER: S-EPMC3545810 | biostudies-other | 2013 Jan

REPOSITORIES: biostudies-other

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Proteome-wide protein interaction measurements of bacterial proteins of unknown function.

Meier Matthias M   Sit Rene V RV   Quake Stephen R SR  

Proceedings of the National Academy of Sciences of the United States of America 20121224 2

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--prote  ...[more]