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Among these, the two most effective suppressors, <jats:italic>sus1<\/jats:italic> and <jats:italic>sus2<\/jats:italic>, resulted from G87D and T55M single amino acid substitutions in HSCA2 (At5g09590) and ISU1 (At4g22220), both crucial components of the mitochondrial iron-sulfur (Fe-S) cluster assembly machinery. SSR1 displayed a robust cochaperone-like activity and interacted with HSCA2 and ISU1, facilitating the binding of HSCA2 to ISU1. In comparison to the wild-type plants, <jats:italic>ssr1-2<\/jats:italic> mutants displayed increased iron accumulation in root tips and altered expression of genes responsive to iron deficiency. Additionally, the enzymatic activities of several iron-sulfur proteins and the mitochondrial membrane potential were reduced in <jats:italic>ssr1-2<\/jats:italic> mutants. Interestingly, <jats:italic>SSR1<\/jats:italic> appears to be exclusive to plant lineages and is induced by environmental stresses. Although HSCA2<jats:sup>G87D<\/jats:sup> and ISU1<jats:sup>T55M<\/jats:sup> can effectively compensate for the phenotypes associated with SSR1 deficiency under favorable conditions, their compensatory effects are significantly diminished under stress. Collectively, SSR1 represents a new and significant component of the mitochondrial Fe-S cluster assembly (ISC) machinery. It may also confer adaptive advantages on plant ISC machinery in response to environmental stress.<\/jats:p>","DOI":"10.1371\/journal.pgen.1011597","type":"journal-article","created":{"date-parts":[[2025,2,5]],"date-time":"2025-02-05T18:39:52Z","timestamp":1738780792000},"page":"e1011597","update-policy":"https:\/\/doi.org\/10.1371\/journal.pgen.corrections_policy","source":"Crossref","is-referenced-by-count":3,"title":["Plant-specific cochaperone SSR1 affects root elongation by modulating the mitochondrial iron-sulfur cluster assembly 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