Cell-free Determination of Binary Complexes That Comprise Extended Protein-Protein Interaction Networks of Yersinia pestis.

ABSTRACT: Binary protein interactions form the basic building blocks of molecular networks and dynamic assemblies that control all cellular functions of bacteria. Although these protein interactions are a potential source of targets for the development of new antibiotics, few high-confidence data sets are available for the large proteomes of most pathogenic bacteria. We used a library of recombinant proteins from the plague bacterium Yersinia pestis to probe planar microarrays of immobilized proteins that represented ∼85% (3552 proteins) of the bacterial proteome, resulting in >77,000 experimentally determined binary interactions. Moderate (K_D ∼μm) to high-affinity (K_D ∼nm) interactions were characterized for >1600 binary complexes by surface plasmon resonance imaging of microa

SUBMITTER: Keasey SL 

PROVIDER: S-EPMC5054345 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature