Figure 3.
Artificial tethering of Mmm1 to mitochondria can rescue loss of ERMES. (A) Schematic of model 3 showing that a Mmm1–Mdm10 dimer is functional upon additional tethering. (B) AlphaFold 3 prediction of Mmm1 and Mdm10 dimer. ChiMERA was added manually along with the ER and OMM. (C) Schematic of constructs used in D. (D) Spot assay of single ERMES deletion yeast expressing artificially tethered ERMES members. Refer to the image caption for details. Panel A: Schematic representation of a functional Mmm1-Mdm10 dimer model facilitated by exogenous tethering. The diagram illustrates the spatial arrangement of the ER, OMM, ChiMERA, Mmm1, and Mdm10. Panel B: AlphaFold3 structural prediction of the Mmm1-Mdm10 heterodimer, with the ER, OMM, and ChiMERA manually modeled for context. Protein structures are color-coded according to prediction confidence levels (pLDDT). Panel C: Structural schematics of the experimental constructs, detailing the fusion of mNG-tagged ERMES subunits (Mmm1, Mdm12, Mdm34) with organelle-targeting sequences (Sec66N and Fis1C). Panel D: Growth phenotypes assessed by spot assay on SD plus FOA medium at 30 degrees Celsius. The assay compares the rescue of mmm1 delta , mdm12 delta, mdm34 delta, and mdm10 delta strains by various mNG-tagged constructs, including wild-type (WT), vector, MMM1-mNG, MDM12-mNG, MDM34-mNG, MMM1-mNG-FIS1C, SEC66N-MDM12-mNG-FIS1C, and SEC66N-MDM34-mNG-FIS1C.

Artificial tethering of Mmm1 to mitochondria can rescue loss of ERMES. (A) Schematic of model 3 showing that a Mmm1–Mdm10 dimer is functional upon additional tethering. (B) AlphaFold 3 prediction of Mmm1 and Mdm10 dimer. ChiMERA was added manually along with the ER and OMM. (C) Schematic of constructs used in D. (D) Spot assay of single ERMES deletion yeast expressing artificially tethered ERMES members.

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