A metabolite binding protein moonlights as a bile-responsive chaperone

ABSTRACT: Bile salts are secreted into the gastrointestinal tract to aid in the absorption of lipids. In addition, bile salts show potent antimicrobial activity in part by mediating bacterial protein unfolding and aggregation. Here, using a protein folding sensor, we made the surprising discovery that the E. coli periplasmic glycerol-3-phosphate (G3P) binding protein UgpB can serve, in absence of its substrate, as a potent molecular chaperone that exhibits anti-aggregation activity against bile salt-induced protein aggregation. The substrate G3P, which is known to accumulate in the later compartments of the digestive system, triggers a functional switch between UgpB's activity as a molecular chaperone and its activity as a G3P transporter. A UgpB mutant unable to bind G3P is constitutively active as

SUBMITTER: Dr. Changhan Lee 

PROVIDER: S-SCDT-EMBOJ-2019-104231 | biostudies-other |

REPOSITORIES: biostudies-other