Chaperone function in Fe-S protein biogenesis: Three possible scenarios

Biochim Biophys Acta Mol Cell Res. 2024 Apr 2:119717. doi: 10.1016/j.bbamcr.2024.119717. Online ahead of print.ABSTRACTAmong the six known iron‑sulfur (FeS) cluster biogenesis machineries that function across all domains of life only one involves a molecular chaperone system. This machinery, called ISC for 'iron sulfur cluster', functions in bacteria and in mitochondria of eukaryotes including humans. The chaperone system - a dedicated J-domain protein co-chaperone termed Hsc20 and its Hsp70 partner - is essential for proper ISC machinery function, interacting with the scaffold protein IscU which serves as a platform for cluster assembly and subsequent transfer onto recipient apo-proteins. Despite many years of research, surprisingly little is known about the specific role(s) that the chaperones play in the ISC machinery. Here we review three non-exclusive scenarios that range from involvement of the chaperones in the cluster transfer to regulation of the cellular levels of IscU itself.PMID:38574821 | DOI:10.1016/j.bbamcr.2024.119717
Source: Biochimica et Biophysica Acta - Category: Biochemistry Authors: Source Type: research