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Essential function of Aco2, a fusion protein of aconitase and mitochondrial ribosomal protein bL21, in mitochondrial translation in fission yeast
Author(s) -
Jung Soo-Jin,
Seo Youngdae,
Lee Kyung-Chang,
Lee Daeyoup,
Roe Jung-Hye
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.02.015
Subject(s) - aconitase , schizosaccharomyces pombe , ribosomal protein , fusion protein , biology , hspa9 , mitochondrial dna , mitochondrion , ribosome , yeast , microbiology and biotechnology , saccharomyces cerevisiae , gene , biochemistry , recombinant dna , peptide sequence , rna
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.