Literature DB >> 25724335

Essential function of Aco2, a fusion protein of aconitase and mitochondrial ribosomal protein bL21, in mitochondrial translation in fission yeast.

Soo-Jin Jung1, Youngdae Seo1, Kyung-Chang Lee1, Daeyoup Lee2, Jung-Hye Roe3.   

Abstract

A possible interaction between aconitase and a mitochondrial ribosomal protein was suggested in a genome-wide interactome study. In fission yeast Schizosaccharomyces pombe, the aco2(+) gene encodes a fusion protein between aconitase and a putative mitochondrial ribosomal protein bL21 (Mrpl49). Two types of aco2(+) transcripts are generated via alternative poly (A) site selection, producing both a single aconitase domain protein and the fusion form. The bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus. The viability defect of aco2 mutation is complemented not by the aconitase domain but by the bL21 domain, which enables mitochondrial translation.
Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Dual function protein; Dual localized protein; Gene fusion; Mitochondrial targeting; Nuclear localization signal; Sub-cellular localization

Mesh:

Substances:

Year:  2015        PMID: 25724335     DOI: 10.1016/j.febslet.2015.02.015

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  10 in total

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2.  Non-mitochondrial aconitase regulates the expression of iron-uptake genes by controlling the RNA turnover process in fission yeast.

Authors:  Soo-Yeon Cho; Soo-Jin Jung; Kyoung-Dong Kim; Jung-Hye Roe
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Authors:  Marie Anne-Catherine Neumann; Dajana Grossmann; Simone Schimpf-Linzenbold; Dana Dayan; Katarina Stingl; Reut Ben-Menachem; Ophry Pines; François Massart; Sylvie Delcambre; Jenny Ghelfi; Jill Bohler; Tim Strom; Amit Kessel; Abdussalam Azem; Ludger Schöls; Anne Grünewald; Bernd Wissinger; Rejko Krüger
Journal:  Sci Rep       Date:  2020-10-07       Impact factor: 4.379

10.  The Mitochondria-to-Cytosol H2O2 Gradient Is Caused by Peroxiredoxin-Dependent Cytosolic Scavenging.

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  10 in total

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