ArticleThe Journal of biological chemistry2011
Mne1 is a novel component of the mitochondrial splicing apparatus responsible for processing of a COX1 group I intron in yeast.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Improvement ofACS synthetic biology · 2020Article
- Synteny-based analyses indicate that sequence divergence is not the main source of orphan genes.eLife · 2020Article
- Unique, Diverged, and Conserved Mitochondrial Functions Influencing Candida albicans Respiration.mBio · 2019Article
- Genome-wide association across Saccharomyces cerevisiae strains reveals substantial variation in underlying gene requirements for toxin tolerance.PLoS genetics · 2018Article
- The evolutionary history of Saccharomyces species inferred from completed mitochondrial genomes and revision in the 'yeast mitochondrial genetic code'.DNA research : an international journal for rapid publication of reports on genes and genomes · 2017Article
- Post-zygotic sterility and cytonuclear compatibility limits in S. cerevisiae xenomitochondrial cybrids.Frontiers in genetics · 2014Article
- Mss116p: a DEAD-box protein facilitates RNA folding.RNA biology · 2013Review
- Two independent activities define Ccm1p as a moonlighting protein in Saccharomyces cerevisiae.Bioscience reports · 2012Article
- Biogenesis and assembly of eukaryotic cytochrome c oxidase catalytic core.Biochimica et biophysica acta · 2012Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Saccharomyces cerevisiae cells lacking Mne1 are deficient in intron splicing in the gene encoding the Cox1 subunit of cytochrome oxidase but contain wild-type levels of the bc(1) complex. Thus, Mne1 has no role in splicing of COB introns or expression of the COB gene. Northern experiments suggest that splicing of the COX1 aI5β intron is dependent on Mne1 in addition to the previously known Mrs1, Mss116, Pet54, and Suv3 factors. Processing of the aI5β intron is similarly impaired in mne1Δ and mrs1Δ cells and overexpression of Mrs1 partially restores the respiratory function of mne1Δ cells. Mrs1 is known to function in the initial transesterification reaction of splicing. Mne1 is a mitochondrial matrix protein loosely associated with the inner membrane and is found in a high mass ribonucleoprotein complex specifically associated with the COX1 mRNA even within an intronless strain. Mne1 does not appear to have a secondary function in COX1 processing or translation, because disruption of MNE1 in cells containing intronless mtDNA does not lead to a respiratory growth defect. Thus, the primary defect in mne1Δ cells is splicing of the aI5β intron in COX1.
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