Post-translocational protein folding in Gram-positive bacteria

NIH RePORTER · NIH · R01 · $89,503 · view on reporter.nih.gov ↗

Abstract

PROJECT SUMMARY The Gram-positive Actinobacteria, including the oral colonizers Actinomyces oris and Corynebacterium matruchotii, as well as the diphtheria-causing pathogen Corynebacterium diphtheriae, employ a disulfide-bond forming machine, MdbA, to promote oxidative protein folding. In A. oris and C. diphtheriae, MdbA catalyzes disulfide bond formation in pilin substrates that are required for oral biofilm formation and polymicrobial interactions. This diversity supplement supports the research training of a graduate student who aims to characterize a conserved membrane protein – working in conjunction with MdbA – that maintains membrane-homoeostasis of an enzyme essential for formation of oral biofilms and polymicrobial interactions. The results generated will advance our understanding of assembly and folding of factors contributing to the development of oral biofilms.

Key facts

NIH application ID
11159227
Project number
3R01DE025015-11S1
Recipient
UNIVERSITY OF CALIFORNIA LOS ANGELES
Principal Investigator
Hung Ton-That
Activity code
R01
Funding institute
NIH
Fiscal year
2024
Award amount
$89,503
Award type
3
Project period
2015-03-01 → 2025-08-31