What is it about?
Assembly of Fe-S clusters is assisted by complex machinery involving an Fe-S scaffold (IscU) and a dedicated chaperone system (HscBA). Here, we identify and characterize mutations in IscU that bypass the otherwise essential in vivo role of HscBA, and show, unlike almost all other proteins, IscU may have to alter its conformation to the denatured state to execute its role.
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This page is a summary of: Evidence for dynamic in vivo interconversion of the conformational states of IscU during iron–sulfur cluster biosynthesis, Molecular Microbiology, December 2020, Wiley,
DOI: 10.1111/mmi.14646.
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