ArticleEukaryotic cell2006
Sequential processing of a mitochondrial tandem protein: insights into protein import in Schizosaccharomyces pombe.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- The cytochrome oxidase defect in ISC-depleted yeast is caused by impaired iron-sulfur cluster maturation of the mitoribosome assembly factor Rsm22.FEBS letters · 2025Article
- The UPRmt preserves mitochondrial import to extend lifespan.The Journal of cell biology · 2022Article
- More than just a ticket canceller: the mitochondrial processing peptidase tailors complex precursor proteins at internal cleavage sites.Molecular biology of the cell · 2020Article
- Redox Regulation of the Mitochondrial Quality Control Protease Oma1.Antioxidants & redox signaling · 2019Article
- Tom70 enhances mitochondrial preprotein import efficiency by binding to internal targeting sequences.The Journal of cell biology · 2018Article
- Ydj1 governs fungal morphogenesis and stress response, and facilitates mitochondrial protein import via Mas1 and Mas2.Microbial cell (Graz, Austria) · 2017Article
- The Assembly Factor Pet117 Couples Heme a Synthase Activity to Cytochrome Oxidase Assembly.The Journal of biological chemistry · 2017Article
- Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein.Molecular biology of the cell · 2016Article
- Review
- Mne1 is a novel component of the mitochondrial splicing apparatus responsible for processing of a COX1 group I intron in yeast.The Journal of biological chemistry · 2011Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sequencing of the genome of Schizosaccharomyces pombe revealed the presence of a number of genes encoding tandem proteins, some of which are mitochondrial components. One of these proteins (pre-Rsm22-Cox11) consists of a fusion of Rsm22, a component of the mitochondrial ribosome, and Cox11, a factor required for copper insertion into cytochrome oxidase. Since in Saccharomyces cerevisiae, Cox11 is physically attached to the mitochondrial ribosome, it was suggested that the tandem organization of Rsm22-Cox11 is used to covalently tie the mitochondrial ribosome to Cox11 in S. pombe. We report here that pre-Rsm22-Cox11 is matured in two subsequent processing events. First, the mitochondrial presequence is removed. At a later stage of the import process, the Rsm22 and Cox11 domains are separated by cleavage of the mitochondrial processing peptidase at an internal processing site. In vivo data obtained using a tagged version of pre-Rsm22-Cox11 confirmed the proteolytic separation of Cox11 from the Rsm22 domain. Hence, the tandem organization of pre-Rsm22-Cox11 does not give rise to a persistent fusion protein but rather might be used to increase the import efficiency of Cox11 and/or to coordinate expression levels of Rsm22 and Cox11 in S. pombe.
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