Yeast aconitase mitochondrial import is modulated by interactions of its C and N terminal domains and Ssa1/2 (Hsp70)

• Main Authors: Ben-Menachem, R, Wang, K, Marcu, O, Yu, Z, Lim, T.K, Lin, Q, Schueler-Furman, O, Pines, O
• Other Authors: MICROBIOLOGY AND IMMUNOLOGY
• Format: Article
• Published: Nature Publishing Group 2020
• Subjects: adenosine triphosphatase; fusion protein; heat shock protein 70; iron regulatory protein 1; protein binding; Saccharomyces cerevisiae protein; SSA1 protein, S cerevisiae; SSA2 protein, S cerevisiae; alpha helix; beta sheet; binding site; chemistry; cytosol; gene expression; gene vector; genetics; metabolism; mitochondrion; molecular model; mutation; protein domain; protein transport; Saccharomyces cerevisiae; Adenosine Triphosphatases; Binding Sites; Cytosol; Gene Expression; Genetic Vectors; HSP70 Heat-Shock Proteins; Iron Regulatory Protein 1; Mitochondria; Models, Molecular; Mutation; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Transport; Recombinant Fusion Proteins; Saccharomyces cerevisiae Proteins
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/174231
• Institution: National University of Singapore

10.1038/s41598-018-24068-w