ArticleThe Journal of cell biology1993
MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- ATF4 regulates mitochondrial dysfunction and mitophagy, contributing to corneal endothelial apoptosis.Scientific reports · 2026Article
- Molecular pathway of mitochondrial preprotein import through the TOM-TIM23 supercomplex.Nature structural & molecular biology · 2023Article
- Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes.eLife · 2022Article
- Article
- Mgr2 regulates mitochondrial preprotein import by associating with channel-forming Tim23 subunit.Molecular biology of the cell · 2020Article
- Role of Tim17 Transmembrane Regions in Regulating the Architecture of Presequence Translocase and Mitochondrial DNA Stability.Molecular and cellular biology · 2017Article
- Molecular insights revealing interaction of Tim23 and channel subunits of presequence translocase.Molecular and cellular biology · 2013Article
- Dual location of the mitochondrial preprotein transporters B14.7 and Tim23-2 in complex I and the TIM17:23 complex in Arabidopsis links mitochondrial activity and biogenesis.The Plant cell · 2012Article
- Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes.The Journal of cell biology · 2012Article
- Lateral release of proteins from the TOM complex into the outer membrane of mitochondria.The EMBO journal · 2011Article
- Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex.Molecular biology of the cell · 2008Article
- A fluorescence assay for peptide translocation into mitochondria.Analytical biochemistry · 2007Article
- A genomewide screen for petite-negative yeast strains yields a new subunit of the i-AAA protease complex.Molecular biology of the cell · 2006Article
- The yeast GTPase Mtg2p is required for mitochondrial translation and partially suppresses an rRNA methyltransferase mutant, mrm2.Molecular biology of the cell · 2005Article
- Proapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids.The Journal of cell biology · 2004Article
- The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria.Molecular biology of the cell · 2003Article
- Possibility of cytoplasmic pre-tRNA splicing: the yeast tRNA splicing endonuclease mainly localizes on the mitochondria.Molecular biology of the cell · 2003Article
- Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane.Molecular biology of the cell · 2003Article
- Tim50, a novel component of the TIM23 preprotein translocase of mitochondria.The EMBO journal · 2003Article
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2 authors.
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Abstract
To identify new components that mediate mitochondrial protein import, we analyzed mas6, an import mutant in the yeast Saccharomyces cerevisiae. mas6 mutants are temperature sensitive for viability, and accumulate mitochondrial precursor proteins at the restrictive temperature. We show that mas6 does not correspond to any of the presently identified import mutants, and we find that mitochondria isolated from mas6 mutants are defective at an early stage of the mitochondrial protein import pathway. MAS6 encodes a 23-kD protein that contains several potential membrane spanning domains, and yeast strains disrupted for MAS6 are inviable at all temperatures and on all carbon sources. The Mas6 protein is located in the mitochondrial inner membrane and cannot be extracted from the membrane by alkali treatment. Antibodies to the Mas6 protein inhibit import into isolated mitochondria, but only when the outer membrane has been disrupted by osmotic shock. Mas6p therefore represents an essential import component located in the mitochondrial inner membrane.
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