Cellular assays identify barriers impeding iron-sulfur enzyme activity in a non-native prokaryotic host.

ABSTRACT: Iron-sulfur (Fe-S) clusters are ancient and ubiquitous protein cofactors and play irreplaceable roles in many metabolic and regulatory processes. Fe-S clusters are built and distributed to Fe-S enzymes by dedicated protein networks. The core components of these networks are widely conserved and highly versatile. However, Fe-S proteins and enzymes are often inactive outside their native host species. We sought to systematically investigate the compatibility of Fe-S networks with non-native Fe-S enzymes. By using collections of Fe-S enzyme orthologs representative of the entire range of prokaryotic diversity, we uncovered a striking correlation between phylogenetic distance and probability of functional expression. Moreover, coexpression of a heterologous Fe-S biogenesis pathway increases th

SUBMITTER: D'Angelo F 

PROVIDER: S-EPMC8896826 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature