HrrSA orchestrates a systemic response to heme and determines prioritization of terminal cytochrome oxidase expression.

ABSTRACT: Heme is a multifaceted molecule. While serving as a prosthetic group for many important proteins, elevated levels are toxic to cells. The complexity of this stimulus has shaped bacterial network evolution. However, only a small number of targets controlled by heme-responsive regulators have been described to date. Here, we performed chromatin affinity purification and sequencing to provide genome-wide insights into in vivo promoter occupancy of HrrA, the response regulator of the heme-regulated two-component system HrrSA of Corynebacterium glutamicum. Time-resolved profiling revealed dynamic binding of HrrA to more than 200 different genomic targets encoding proteins associated with heme biosynthesis, the respiratory chain, oxidative stress response and cell envelope remodeling. By repress

SUBMITTER: Keppel M 

PROVIDER: S-EPMC7337898 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature