DOI: 10.5061/dryad.2ngf1vj0c
title: Network of Dmo2p interactors through mass spectrometry analyses of proteins differentially purified from the PC beads in the DMO2-PC strain

description: Based on available platforms detailing the Saccharomyces cerevisiae
 mitochondrial proteome and other high-throughput studies, we identified
 the yeast gene DMO2 as having a profile of genetic and physical
 interactions that indicate a putative role in mitochondrial respiration.
 Dmo2p is a homolog to human distal membrane-arm assembly complex protein 1
 (DMAC1); both proteins have two conserved cysteines in a Cx2C motif. Here,
 we localized Dmo2p in the mitochondrial inner membrane with the conserved
 cysteines facing the intermembrane space. The respiratory deficiency of
 dmo2 mutants at 37oC led to a reduction in cytochrome c oxidase (COX)
 activity (COX) and in the formation of cytochrome bc1 complex–COX
 supercomplexes; dmo2 also has a rapid turnover of Cox2p, the second
 subunit of the COX complex that harbors the binuclear CuA center.
 Moreover, Dmo2p co-immunoprecipitates with Cox2p and components required
 for maturation of the CuA center, such as Sco1p and Sco2p. Finally, DMO2
 overexpression can suppress cox23 respiratory deficiency, a mutant that
 has impaired mitochondrial copper homeostasis. Mass spectrometry data
 unveiled the interaction of Dmo2p with different large molecular
 complexes, including bc1–COX supercomplexes, the TIM23 machinery, and the
 ADP/ATP nucleotide translocator. Overall, our data suggest that Dmo2p is
 required for Cox2p maturation, potentially by aiding proteins involved in
 copper transport and incorporation into Cox2p
description: Protein quantification was conducted utilising the MaxQuant
 label‐free algorithm (LFQ), which employed unique and razor peptides for
 accurate measurement. A minimum requirement of ≥ 2 ratio counts was set as
 essential for valid protein quantification. Mass
 spectrometry analyses were performed at the Redox Proteomics Core of the
 Mass Spectrometry Resource at Chemistry Institute, University of São
 Paulo; the results were processed using the perseus software suite. Data
 were transformed [log2(x)] and filtered so that for each protein, at least
 one group (Dmo2‐PC/wild‐type) contained a minimum of 50% valid values.
 Subsequent steps in perseus included a two‐sample t‐test to compare the
 means of the label‐free quantitation (LFQ) intensity values between the
 Dmo2‐PC and wild‐type groups.
description: # Network of Dmo2p interactors through mass spectrometry analyses of
 proteins differentially purified from the PC beads in the DMO2-PC strain
 [https://doi.org/10.5061/dryad.2ngf1vj0c](https://doi.org/10.5061/dryad.2ngf1vj0c) ## Description of the data and file structure DMO2-PC interactome data:  Dmo2p interactors were unveiled through mass spectrometry analyses of proteins differentially purified from PC beads in a yeast strain harboring the DMO2‐PC construct. The xlsx file  (EXCEL) contains the list of proteins enriched in DMO2-CH  pull down vs. the wild type and a second control protein. The "difference" values represent the obtained enrichment number for the identified protein in the DMO2-CH pull-down vs the control. Protein IDs, Protein names, and Gene names are indicated.