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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
gene expression
gene vector
molecular model
protein domain
protein transport
Saccharomyces cerevisiae
Adenosine Triphosphatases
Binding Sites
Gene Expression
Genetic Vectors
HSP70 Heat-Shock Proteins
Iron Regulatory Protein 1
Models, Molecular
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.
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
ISSN: 2045-2322
DOI: 10.1038/s41598-018-24068-w
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