Dataset Information
The SlyD metallochaperone targets iron-sulfur biogenesis pathways and the TCA cycle.
Ontology highlight
ABSTRACT: Importance
Correct folding of proteins represents a crucial step for their functions. Among the chaperones that control protein folding, the ubiquitous PPIases catalyze the cis/trans-isomerization of peptidyl-prolyl bonds. Only few protein targets of PPIases have been reported in bacteria. To fill this knowledge gap, we performed a large-scale two-hybrid screen to search for targets of the Escherichia coli and Helicobacter pylori SlyD PPIase-metallochaperone. SlyD from both organisms interacts with enzymes (i) containing metal cofactors, (ii) from the central metabolism tricarboxylic acid (TCA) cycle, and (iii) involved in the formation of the essential and ancestral Fe-S cluster cofactor. E. coli and H. pylori ∆slyD mutants present similar phenotypes of diminished susceptibility to antibiotics and to oxidative stress. In H. pylori, measurements of the intracellular ATP content, proton motive force, and activity of TCA cycle proteins suggest that SlyD regulates TCA cycle enzymes by controlling the formation of their indispensable Fe-S clusters.
SUBMITTER: Denic M
PROVIDER: S-EPMC10653786 | biostudies-literature | 2023 Oct
REPOSITORIES: biostudies-literature
Publications
The SlyD metallochaperone targets iron-sulfur biogenesis pathways and the TCA cycle.
mBio 20230816 5
<h4>Importance</h4>Correct folding of proteins represents a crucial step for their functions. Among the chaperones that control protein folding, the ubiquitous PPIases catalyze the <i>cis</i>/<i>trans</i>-isomerization of peptidyl-prolyl bonds. Only few protein targets of PPIases have been reported in bacteria. To fill this knowledge gap, we performed a large-scale two-hybrid screen to search for targets of the <i>Escherichia coli</i> and <i>Helicobacter pylori</i> SlyD PPIase-metallochaperone. ...[more]