Protein-protein interactions are pivotal in many biological processes and essential for a global understanding of cell functions. In the present study, we combined 2-D native/SDS-PAGE-based proteomics with Co-immunoprecipitation, far-Western blotting, His-tag affinity purification and functional analysis to establish a reference map of E. coli cytosolic complexome. The reference map included 23 distinct heteromeric and 22 homomeric protein complexes. These complexes mainly contributed to glycolysis/gluconeogenesis, information processing and cellular processes. Out of these complexes, 8 heteromeric and 1 homomeric protein complexes were responsible for baloxin resistance. Functions of these complexes in response to the resistance were categorized into information streams, monosaccharide metabolism, response to stimulus and amino acid metabolic process. Out of them, these complexes contributing to information streams and response to stimulus played a key role in the resistance in comparison with those in response to ceftriaxone, which worked for monosaccharide metabolic process. The results renew the understanding of the acquired quinolone-resistant mechanism that is attributed to GyrA-GyrB complex, indicating DNA metabolic process and translational elongation of the information streams and response to stimulus are also responsible for the resistance. These findings highlight the study of antibiotic-resistant mechanisms.
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