Functional and structural characterization of Hyp730, a highly conserved and dormancy ‐specific hypothetical membrane protein

Dormancy requires a bacterium to be tolerant to external stresses, including antibiotics, hypoxia, nutrient deprivation, or immune surveillance from the host organism. Dormant bacteria aim to survive by minimizing their biological events, such as by adopting a state of non ‐replicative persistence, yet the molecular mechanism and protein which regulates dormancy are largely unknown. Here, we identified inMicrococcus luteus a dormancy ‐specific protein, Hyp730 is a membrane protein, widely conserved across Actinobacteria includingMycobacterium tuberculosis, but whose biological function has remained elusive. We determined its structural properties which suggest Hyp730 ‐like proteins are involved in efficient respiration events. Strategies to suppress the function of Hyp730 may represent new therapeutic approaches for inhibiting virulence against pathogens that persist under stress conditions. AbstractMembrane proteins represent major drug targets, and the ability to determine their functions, structures, and conformational changes will significantly advance mechanistic approaches to both biotechnology and bioremediation, as well as the fight against pathogenic bacteria. A pertinent example isMycobacterium tuberculosis (H37Rv), which contains ~4000 protein ‐coding genes, with almost a thousand having been categorized as ‘membrane protein’, and a few of which (~1%) have been functionally characterized and structurally modeled. However, the functions and structures of...
Source: MicrobiologyOpen - Category: Microbiology Authors: Tags: ORIGINAL ARTICLE Source Type: research