The Aconitase C-Terminal Domain Is an Independent Dual Targeting Element

Ben-Menachem, Reut; Regev‐Rudzki, Neta; Pines, Ophry

doi:10.1016/j.jmb.2011.03.045

Cited by 16 publications

(13 citation statements)

References 31 publications

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“…A reported example of a dually targeted enzyme that displays distinct functions in the different compartments has been described for the yeast aconitase 1, which localizes to both mitochondria and the cytosol (50,63). Interestingly, as demonstrated in this study for Pink1, the C terminus of aconitase 1 serves as a targeting element, and it contributes to the dual localization of the enzyme (64).…”

Section: Discussionsupporting

confidence: 55%

Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode

Becker

Richter

Tocilescu

et al. 2012

Journal of Biological Chemistry

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Background:The Parkinson-related kinase Pink1 is implicated in mitochondrial quality control. Results: Integration of multiple targeting signals results in the localization of Pink1 and its processing product to the surface of the outer membrane. Conclusion: Pink1 follows a unique import pathway that allows probing the functional integrity of mitochondria. Significance: Determining the Pink1 targeting mode provides the basis for defining its molecular function.

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Section: Discussionsupporting

confidence: 55%

Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode

Becker

Richter

Tocilescu

et al. 2012

Journal of Biological Chemistry

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“…5). It has been shown recently that the two mitochondrial enzymes fumarase and aconitase play a minor function in the nucleus that becomes essential under DNA-damaging conditions (Yogev et al, 2010; Ben-Menachem et al, 2011). Our findings would indicate that such cases may be much more prevalent than previously appreciated.…”

Section: Resultsmentioning

confidence: 99%

A novel single-cell screening platform reveals proteome plasticity during yeast stress responses

Breker

Gymrek

Schuldiner

2013

Journal of Cell Biology

214

200

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“…Fusion of this C-terminal domain to mitochondria-targeted passenger-proteins, such as orotidine-5′-phosphate decarboxylase and dihydrofolate-reductase, conferred on them eclipsed dual localization. Thus, the aconitase C-terminal domain serves as an “independent signal” which is on the one hand necessary and sufficient for dual targeting on the other 17 .…”

Section: Introductionmentioning

confidence: 99%

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

Ben-Menachem

Wang

Marcu

et al. 2018

Sci Rep

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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).

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The Aconitase C-Terminal Domain Is an Independent Dual Targeting Element

Cited by 16 publications

References 31 publications

Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode

Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode

A novel single-cell screening platform reveals proteome plasticity during yeast stress responses

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

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