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

Reut Ben-Menachem, Katherine Wang, Orly Marcu, Zhang Yu, Teck Kwang Lim, Qingsong Lin, Ora Schueler-Furman, Ophry Pines*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


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).

Original languageAmerican English
Article number5903
JournalScientific Reports
Issue number1
StatePublished - 1 Dec 2018

Bibliographical note

Funding Information:
This work was supported by grants to O. Pines from the Israel Science Foundation (ISF), the German Israeli Project Cooperation (DIP), the CREATE Project of the National Research Foundation of Singapore and the Pakula Family (via the American Friends of the Hebrew University). R. Ben-Menachem was supported by the Eliyahu Pen Dedicated Fund.

Publisher Copyright:
© 2018 The Author(s).


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