Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-018-24068-w
Title: Yeast aconitase mitochondrial import is modulated by interactions of its C and N terminal domains and Ssa1/2 (Hsp70)
Authors: Ben-Menachem, R
Wang, K
Marcu, O
Yu, Z 
Lim, T.K 
Lin, Q 
Schueler-Furman, O
Pines, O 
Keywords: 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
Saccharomyces cerevisiae Proteins
Issue Date: 2018
Publisher: Nature Publishing Group
Citation: Ben-Menachem, R, Wang, K, Marcu, O, Yu, Z, Lim, T.K, Lin, Q, Schueler-Furman, O, Pines, O (2018). Yeast aconitase mitochondrial import is modulated by interactions of its C and N terminal domains and Ssa1/2 (Hsp70). Scientific Reports 8 (1) : 5903. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-018-24068-w
Abstract: Molecules of single proteins, echoforms, can be distributed between two (or more) subcellular locations, a phenomenon which we refer to as dual targeting or dual localization. The yeast aconitase gene ACO1 (778 amino acids), encodes a single translation product that is nonetheless dual localized to the cytosol and mitochondria by a reverse translocation mechanism. The solved crystal structure of aconitase isolated from porcine heart mitochondria shows that it has four domains. The first three tightly associated N-terminal domains are tethered to the larger C-terminal fourth domain (C-terminal amino acids 517-778). We have previously shown that the aconitase C terminal domain constitutes an independent dual targeting signal when fused to mitochondria-targeted passenger-proteins. We show that the aconitase N and C-terminal domains interact and that this interaction is important for efficient aconitase post translational import into mitochondria and for aconitase dual targeting (relative levels of aconitase echoforms). Our results suggest a "chaperone-like function" of the C terminal domain towards the N terminal domains which can be modulated by Ssa1/2 (cytosolic Hsp70). © 2018 The Author(s).
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/174231
ISSN: 2045-2322
DOI: 10.1038/s41598-018-24068-w
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