TusA influences Fe-S cluster assembly and iron homeostasis in E. coli by reducing the translation efficiency of Fur.

ABSTRACT: All sulfur transfer pathways have generally a l-cysteine desulfurase as an initial sulfur-mobilizing enzyme in common, which serves as a sulfur donor for the biosynthesis of numerous sulfur-containing biomolecules in the cell. In Escherichia coli, the housekeeping l-cysteine desulfurase IscS has several interaction partners, which bind at different sites of the protein. So far, the interaction sites of IscU, Fdx, CyaY, and IscX involved in iron-sulfur (Fe-S) cluster assembly have been mapped, in addition to TusA, which is required for molybdenum cofactor biosynthesis and mnm⁵s²U34 tRNA modifications, and ThiI, which is involved in thiamine biosynthesis and s⁴U8 tRNA modifications. Previous studies predicted that the sulfur acceptor proteins bind to I

SUBMITTER: Olivieri P 

PROVIDER: S-EPMC11302051 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature