ERG6 (YML008C) encodes S-adenosyl-L-methionine:Delta24-sterol C-methyltransferase (SMT, EC 2.1.1.41) of Saccharomyces cerevisiae, which transfers a methyl group from SAM to C-24 of zymosterol to form fecosterol, introducing the C-28 methyl group that distinguishes ergosterol from cholesterol. Erg6 is a Rossmann-fold class I SAM-dependent methyltransferase with a sterol methyltransferase C-terminal domain; photoaffinity labelling of the recombinant enzyme defined its AdoMet-binding segment (residues 120-134). Erg6 is a peripheral, monotopic protein that is found mainly on lipid droplets, where it is enzymatically active and is a standard lipid-droplet marker, with a smaller ER pool enriched in plasma-membrane-associated ER. erg6 null mutants make no ergosterol but grow vegetatively on unmethylated sterol intermediates; they show pleiotropic membrane defects including nystatin resistance, cycloheximide and drug hypersensitivity, poor transformation, defective mating and tryptophan uptake.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003838 sterol 24-C-methyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PANTHER IBA for the sterol 24-C-methyltransferase node (PTN002226525; Arabidopsis SMT1, Candida ERG6, S. cerevisiae Erg6). Erg6 is the experimentally characterised fungal SMT; core function. Supporting Evidence: PMID:6363386 Various nystatin-resistant mutants defective in S-adenosylmethionine: delta 24-sterol-C-methyltransferase (EC 2.1.1.41) were shown to possess alleles of the same gene, erg6. file:yeast/ERG6/ERG6-uniprot.txt Reaction=zymosterol + S-adenosyl-L-methionine = fecosterol + S- |
| GO:0003838 sterol 24-C-methyltransferase activity | IDA PMID:18563465 Photoaffinity labeling and mutational analysis of 24-C-stero... | ACCEPT | Summary: Jayasimha & Nes 2008 assayed recombinant S. cerevisiae SMT (Erg6p), photolabelled it with [3H]AdoMet and analysed active-site mutants kinetically. Direct biochemical evidence for the methyltransferase activity. Supporting Evidence: PMID:18563465 Photolabeling and site-directed mutagenesis were performed on recombinant Saccharomyces cerevisiae 24-C-sterol methyltransferase (SMT) to elucidate the location and role of active site residues involved in AdoMet binding and catalysis. PMID:18563465 The results indicate that one or both of Cys128 and Pro133 are covalently bound to AdoMet. |
| GO:0003838 sterol 24-C-methyltransferase activity | IDA PMID:6363386 Sterol methylation in Saccharomyces cerevisiae. | ACCEPT | Summary: McCammon et al. 1984 showed erg6 mutants are defective in SAM:Delta24-sterol C-methyltransferase activity (EC 2.1.1.41) and measured the activity in subcellular fractions. Core activity. Supporting Evidence: PMID:6363386 Various nystatin-resistant mutants defective in S-adenosylmethionine: delta 24-sterol-C-methyltransferase (EC 2.1.1.41) were shown to possess alleles of the same gene, erg6. PMID:6363386 Despite the single locus for erg6, S-adenosylmethionine: delta 24-sterol-C-methyltransferase enzyme activity was found in three separate fractions: mitochondria, microsomes, and the "floating lipid layer." |
| GO:0003838 sterol 24-C-methyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (ARBA, RHEA:21128, EC 2.1.1.41). Correct reaction (zymosterol -> fecosterol) for Erg6. Supporting Evidence: file:yeast/ERG6/ERG6-uniprot.txt Reaction=zymosterol + S-adenosyl-L-methionine = fecosterol + S- |
| GO:0003838 sterol 24-C-methyltransferase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (ERGOSTEROL-SYN-PWY-1) for zymosterol + SAM -> fecosterol + SAH; correct reaction. Supporting Evidence: PMID:6363386 Various nystatin-resistant mutants defective in S-adenosylmethionine: delta 24-sterol-C-methyltransferase (EC 2.1.1.41) were shown to possess alleles of the same gene, erg6. file:yeast/ERG6/ERG6-uniprot.txt Reaction=zymosterol + S-adenosyl-L-methionine = fecosterol + S- |
| GO:0003838 sterol 24-C-methyltransferase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (PWY-6075-1) for the same C-24 methylation step; correct. Supporting Evidence: PMID:6363386 Various nystatin-resistant mutants defective in S-adenosylmethionine: delta 24-sterol-C-methyltransferase (EC 2.1.1.41) were shown to possess alleles of the same gene, erg6. |
| GO:0003838 sterol 24-C-methyltransferase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (PWY3O-31704 superpathway) for the same step; correct. Supporting Evidence: PMID:6363386 Various nystatin-resistant mutants defective in S-adenosylmethionine: delta 24-sterol-C-methyltransferase (EC 2.1.1.41) were shown to possess alleles of the same gene, erg6. |
| GO:0005739 mitochondrion | EXP PMID:6363386 Sterol methylation in Saccharomyces cerevisiae. | MARK AS OVER ANNOTATED | Summary: McCammon et al. 1984 detected SMT activity in a mitochondrial fraction (as well as microsomes and the floating lipid layer), but note that the distribution between fractions depended on assay conditions. Later work shows Erg6 is mainly on lipid droplets with an ER pool; the mitochondrial signal is likely contact-site co-fractionation. The fractionation result is not disputed, but as a statement of Erg6's location it over-reaches. Supporting Evidence: PMID:6363386 Despite the single locus for erg6, S-adenosylmethionine: delta 24-sterol-C-methyltransferase enzyme activity was found in three separate fractions: mitochondria, microsomes, and the "floating lipid layer." PMID:6363386 The amount of activity in each fraction could be manipulated by assay conditions. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. |
| GO:0005739 mitochondrion | HDA PMID:14576278 The proteome of Saccharomyces cerevisiae mitochondria. | MARK AS OVER ANNOTATED | Summary: High-throughput mitochondrial proteomics (Sickmann et al. 2003 mitochondrial proteome) detected Erg6. Erg6 is an ER/lipid-droplet enzyme that is abundant and enriched in ER subdomains closely apposed to other organelles; detection in purified mitochondria most plausibly reflects ER/lipid-droplet co-purification at contact sites rather than a mitochondrial pool with a distinct function. Not wrong as a fractionation result, but an over-annotation of the protein's location. Supporting Evidence: PMID:14576278 The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. PMID:24868093 Sec61 and Erg6 are negative and positive controls, respectively. |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | MARK AS OVER ANNOTATED | Summary: High-throughput mitochondrial proteomics (Reinders et al. 2006 PROMITO dataset) detected Erg6. Erg6 is an ER/lipid-droplet enzyme that is abundant and enriched in ER subdomains closely apposed to other organelles; detection in purified mitochondria most plausibly reflects ER/lipid-droplet co-purification at contact sites rather than a mitochondrial pool with a distinct function. Not wrong as a fractionation result, but an over-annotation of the protein's location. Supporting Evidence: PMID:16823961 A total of 851 different proteins (PROMITO dataset) were identified by use of multidimensional LC-MS/MS PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. PMID:24868093 Sec61 and Erg6 are negative and positive controls, respectively. |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | MARK AS OVER ANNOTATED | Summary: High-throughput mitochondrial proteomics (Renvoise et al. 2014 quantitative mitochondrial proteome) detected Erg6. Erg6 is an ER/lipid-droplet enzyme that is abundant and enriched in ER subdomains closely apposed to other organelles; detection in purified mitochondria most plausibly reflects ER/lipid-droplet co-purification at contact sites rather than a mitochondrial pool with a distinct function. Not wrong as a fractionation result, but an over-annotation of the protein's location. Supporting Evidence: PMID:24769239 we performed an overall quantitative proteomic and phosphoproteomic study of isolated mitochondria extracted from yeast grown on fermentative (glucose or galactose) and respiratory (lactate) media. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. PMID:24868093 Sec61 and Erg6 are negative and positive controls, respectively. |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | MARK AS OVER ANNOTATED | Summary: UniProt SubCell mapping (SL-0173); UniProt lists Mitochondrion citing McCammon et al. 1984 fractionation only. Lipid droplet, the best-supported location, is missing from that UniProt entry. The mitochondrial assignment is an over-statement of a fractionation result. Supporting Evidence: file:yeast/ERG6/ERG6-uniprot.txt Mitochondrion {ECO:0000269|PubMed:6363386}. PMID:6363386 The amount of activity in each fraction could be manipulated by assay conditions. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. |
| GO:0005741 mitochondrial outer membrane | HDA PMID:16407407 Proteomic analysis of the yeast mitochondrial outer membrane... | MARK AS OVER ANNOTATED | Summary: Zahedi et al. 2006 mitochondrial outer membrane proteome. Erg6 has no transmembrane segment or outer-membrane targeting information and is a lipid-droplet/ER enzyme; its detection is best explained by co-purification of LD/ER contacts with outer membranes (the authors themselves note unexpected proteins in this proteome). Supporting Evidence: PMID:16407407 Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. PMID:24868093 Sec61 and Erg6 are negative and positive controls, respectively. |
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: PANTHER IBA (PTN002226525) for ER, is_active_in. Erg6 is active in microsomes as well as lipid droplets, so an ER activity site is supported. Supporting Evidence: PMID:6363386 Despite the single locus for erg6, S-adenosylmethionine: delta 24-sterol-C-methyltransferase enzyme activity was found in three separate fractions: mitochondria, microsomes, and the "floating lipid layer." PMID:11298754 several enzymes involved in ergosterol biosynthesis, namely squalene synthase (Erg9p), squalene epoxidase (Erg1p) and steroldelta24-methyltransferase (Erg6p), are highly enriched in PAM. |
| GO:0005783 endoplasmic reticulum | IDA PMID:11298754 A subfraction of the yeast endoplasmic reticulum associates ... | ACCEPT | Summary: Pichler et al. 2001 found Erg6p highly enriched in the plasma-membrane-associated ER subfraction (PAM), a lipid-synthesising ER domain. Supporting Evidence: PMID:11298754 several enzymes involved in ergosterol biosynthesis, namely squalene synthase (Erg9p), squalene epoxidase (Erg1p) and steroldelta24-methyltransferase (Erg6p), are highly enriched in PAM. |
| GO:0005783 endoplasmic reticulum | IDA PMID:6363386 Sterol methylation in Saccharomyces cerevisiae. | ACCEPT | Summary: McCammon et al. 1984 measured SMT activity in microsomes; supports is_active_in ER. Supporting Evidence: PMID:6363386 Despite the single locus for erg6, S-adenosylmethionine: delta 24-sterol-C-methyltransferase enzyme activity was found in three separate fractions: mitochondria, microsomes, and the "floating lipid layer." file:yeast/ERG6/ERG6-uniprot.txt SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:6363386}. |
| GO:0005783 endoplasmic reticulum | IDA PMID:9450962 Dual localization of squalene epoxidase, Erg1p, in yeast ref... | ACCEPT | Summary: Leber et al. 1998 used Erg6p as a comparison for Erg1p distribution, finding it mainly in lipid particles; the curator assigned the minor ER pool from this fractionation. Accepted as a secondary location. Supporting Evidence: PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. |
| GO:0005811 lipid droplet | IDA PMID:10515935 Identification and characterization of major lipid particle ... | ACCEPT | Summary: Athenstaedt et al. 1999 identified Erg6p as a major lipid-particle protein and note it is enzymatically active in lipid particle preparations. Lipid droplet is the principal location of Erg6. Supporting Evidence: PMID:10515935 This is very likely for Erg6p ( 27 ) and Erg7p ( 4a ), which are enzymatically active in lipid particle preparations. PMID:10515935 This approach supported previous findings concerning the localization of Erg6p and Erg1p to lipid particles |
| GO:0005811 lipid droplet | IDA PMID:24868093 High confidence proteomic analysis of yeast LDs identifies a... | ACCEPT | Summary: Currie et al. 2014 high-confidence LD proteome detected Erg6, and used Erg6-GFP as the positive control for LD co-localisation. Supporting Evidence: PMID:24868093 Sec61 and Erg6 are negative and positive controls, respectively. PMID:24868093 Twelve proteins (Ayr1, Eht1, Erg1, Erg6, Erg7, Faa1, Faa4, Fat1, Pet10, Slc1, Tgl1, and Tgl3) were detected in the current work and all reported proteomes. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | MODIFY | Summary: YeastPathways RCA (ERGOSTEROL-SYN-PWY-1) default cytosol compartment. Erg6 is a membrane-associated enzyme acting on membrane sterols and is found on lipid droplets and the ER, not free in the cytosol. Proposed replacements: lipid droplet endoplasmic reticulum Supporting Evidence: PMID:10515935 This is very likely for Erg6p ( 27 ) and Erg7p ( 4a ), which are enzymatically active in lipid particle preparations. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. PMID:11298754 several enzymes involved in ergosterol biosynthesis, namely squalene synthase (Erg9p), squalene epoxidase (Erg1p) and steroldelta24-methyltransferase (Erg6p), are highly enriched in PAM. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | MODIFY | Summary: YeastPathways RCA (PWY-6075-1) default cytosol compartment; Erg6 is active on lipid droplets and in the ER. Proposed replacements: lipid droplet endoplasmic reticulum Supporting Evidence: PMID:10515935 This is very likely for Erg6p ( 27 ) and Erg7p ( 4a ), which are enzymatically active in lipid particle preparations. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. PMID:11298754 several enzymes involved in ergosterol biosynthesis, namely squalene synthase (Erg9p), squalene epoxidase (Erg1p) and steroldelta24-methyltransferase (Erg6p), are highly enriched in PAM. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | MODIFY | Summary: YeastPathways RCA (PWY3O-31704 superpathway) default cytosol compartment; Erg6 is active on lipid droplets and in the ER. Proposed replacements: lipid droplet endoplasmic reticulum Supporting Evidence: PMID:10515935 This is very likely for Erg6p ( 27 ) and Erg7p ( 4a ), which are enzymatically active in lipid particle preparations. PMID:9450962 sterol Delta24-methyltransferase (Erg6p), an enzyme catalyzing a late step in sterol biosynthesis, was found mainly in lipid particles cofractionating with triacylglycerols and steryl esters. PMID:11298754 several enzymes involved in ergosterol biosynthesis, namely squalene synthase (Erg9p), squalene epoxidase (Erg1p) and steroldelta24-methyltransferase (Erg6p), are highly enriched in PAM. |
| GO:0006694 steroid biosynthetic process | IEA GO_REF:0000002 | MODIFY | Summary: InterPro IPR013705 (sterol methyltransferase C-terminal domain) mapping to the generic steroid biosynthetic process; correct but unspecific. Erg6 acts in ergosterol biosynthesis. Proposed replacements: ergosterol biosynthetic process Supporting Evidence: PMID:6363386 No ergosterol (C28 sterol) could be detected in whole-cell sterol extracts of the erg6 mutants PMID:2677674 ERG6, the putative structural gene for S-adenosylmethionine: delta 24-methyltransferase, which catalyzes C-24 methylation, was cloned |
| GO:0006696 ergosterol biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: PANTHER IBA (PTN000802684) for ergosterol biosynthesis, seeded by Candida ERG6, S. pombe erg6 and S. cerevisiae Erg6. Supporting Evidence: PMID:6363386 No ergosterol (C28 sterol) could be detected in whole-cell sterol extracts of the erg6 mutants |
| GO:0006696 ergosterol biosynthetic process | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA IEA for ergosterol biosynthetic process; correct for Erg6. Supporting Evidence: file:yeast/ERG6/ERG6-uniprot.txt zymosterol: step 1/5. {ECO:0000269|PubMed:6363386}. |
| GO:0006696 ergosterol biosynthetic process | IMP PMID:2677674 The yeast gene ERG6 is required for normal membrane function... | ACCEPT | Summary: Gaber et al. 1989: erg6 null cells cannot methylate ergosterol precursors at C-24 (IMP). Ergosterol cannot be formed without the C-28 methyl group. Supporting Evidence: PMID:2677674 Although erg6 delta cells are unable to methylate ergosterol precursors at C-24, they exhibit normal vegatative growth, suggesting that C-28 sterols are not essential in S. cerevisiae. PMID:2677674 ERG6, the putative structural gene for S-adenosylmethionine: delta 24-methyltransferase, which catalyzes C-24 methylation, was cloned |
| GO:0006696 ergosterol biosynthetic process | IMP PMID:6363386 Sterol methylation in Saccharomyces cerevisiae. | ACCEPT | Summary: McCammon et al. 1984: erg6 mutants contain no detectable ergosterol (IMP). Supporting Evidence: PMID:6363386 No ergosterol (C28 sterol) could be detected in whole-cell sterol extracts of the erg6 mutants |
| GO:0006696 ergosterol biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (ERGOSTEROL-SYN-PWY-1); correct process. Supporting Evidence: PMID:6363386 No ergosterol (C28 sterol) could be detected in whole-cell sterol extracts of the erg6 mutants |
| GO:0006696 ergosterol biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (PWY-6075-1); correct process. Supporting Evidence: PMID:6363386 No ergosterol (C28 sterol) could be detected in whole-cell sterol extracts of the erg6 mutants |
| GO:0006696 ergosterol biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (PWY3O-31704 superpathway); correct process, Erg6 is a genuine pathway enzyme. Supporting Evidence: PMID:6363386 No ergosterol (C28 sterol) could be detected in whole-cell sterol extracts of the erg6 mutants |
| GO:0008168 methyltransferase activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro (IPR013705/IPR030384) mapping to generic methyltransferase activity; correct class but Erg6's specific activity is sterol 24-C-methyltransferase. Proposed replacements: sterol 24-C-methyltransferase activity Supporting Evidence: PMID:18563465 Photolabeling and site-directed mutagenesis were performed on recombinant Saccharomyces cerevisiae 24-C-sterol methyltransferase (SMT) to elucidate the location and role of active site residues involved in AdoMet binding and catalysis. file:yeast/ERG6/ERG6-uniprot.txt Reaction=zymosterol + S-adenosyl-L-methionine = fecosterol + S- |
| GO:0008757 S-adenosylmethionine-dependent methyltransferase activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro IPR013216 (Methyltransf_11, SAM-dependent MTase domain) mapping. True (GO:0008757 is a direct parent of GO:0003838) and supported by the AdoMet photolabelling, but the specific activity term should be used. Proposed replacements: sterol 24-C-methyltransferase activity Supporting Evidence: PMID:18563465 Photolabeling and site-directed mutagenesis were performed on recombinant Saccharomyces cerevisiae 24-C-sterol methyltransferase (SMT) to elucidate the location and role of active site residues involved in AdoMet binding and catalysis. PMID:18563465 The results indicate that one or both of Cys128 and Pro133 are covalently bound to AdoMet. |
| GO:0016126 sterol biosynthetic process | IEA GO_REF:0000041 | MODIFY | Summary: UniPathway UPA00768 mapping to sterol biosynthetic process; correct but parent of the more specific ergosterol biosynthetic process already annotated. Proposed replacements: ergosterol biosynthetic process Supporting Evidence: file:yeast/ERG6/ERG6-uniprot.txt zymosterol: step 1/5. {ECO:0000269|PubMed:6363386}. |
| GO:0042802 identical protein binding | IPI PMID:16300994 A systematic study of yeast sterol biosynthetic protein-prot... | KEEP AS NON CORE | Summary: Mo & Bard 2005 split-ubiquitin screen of sterol biosynthetic enzymes detected Erg6 self-interaction. Self-association is plausible for SMTs but its functional relevance has not been shown; retained as non-core. Supporting Evidence: PMID:16300994 We employed a split-ubiquitin membrane protein yeast two-hybrid system to characterize interactions between sterol biosynthetic proteins. |
| GO:0042802 identical protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | KEEP AS NON CORE | Summary: Yu et al. 2008 high-quality Y2H interactome detected an Erg6-Erg6 interaction. Independent support for self-association; functional significance unknown. Supporting Evidence: PMID:18719252 we developed an empirically controlled mapping framework to produce a "second-generation" high-quality, high-throughput Y2H data set |
| GO:0042802 identical protein binding | IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i... | KEEP AS NON CORE | Summary: Marchant et al. 2019 DHFR-PCA survey of homomers and paralog heteromers detected an Erg6 homomer in vivo; third independent method. Non-core. Supporting Evidence: PMID:31454312 We refer to these complexes as homomers (HMs) and heteromers of paralogs (HETs). |
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Download this section (compressed HTML)Q: Is the lipid-droplet pool of Erg6 the main site of zymosterol methylation in vivo, or is the ER pool (where downstream Erg2/Erg3/Erg5/Erg4 act) the physiologically dominant one?
Experiment: Anchor Erg6 exclusively to the ER or to lipid droplets (e.g. with compartment-specific membrane anchors) and quantify fecosterol/ergosterol flux to test which pool supports ergosterol synthesis.
Delta(24)-sterol C-methyltransferase; converts zymosterol to fecosterol in the ergosterol biosynthetic pathway by methylating position C-24; localized to lipid particles, the plasma membrane-associated endoplasmic reticulum, and the mitochondrial outer membrane
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