Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway.

ABSTRACT: All sulfur transfer pathways generally have in common an l-cysteine desulfurase as the initial sulfur-mobilizing enzyme, 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 functions as a hub for sulfur transfer through interactions with several partner proteins, which bind at different sites on IscS. So far, the interaction sites of IscU, Fdx, CyaY, and IscX involved in iron sulfur (Fe-S) cluster assembly, TusA, required for molybdenum cofactor biosynthesis and mnm⁵s²U34 transfer RNA (tRNA) modifications, and ThiI, involved in both the biosynthesis of thiamine and s⁴U8 tRNA modifications, have been mapped. Previous studies have s

SUBMITTER: Olivieri P 

PROVIDER: S-EPMC11302665 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature