Comprehensive Proteomic Analysis of PGC7-Interacting Proteins

J Proteome Res. 2017 Sep 1;16(9):3113-3123. doi: 10.1021/acs.jproteome.6b00883. Epub 2017 Aug 2.


Primordial germ cell 7 (PGC7), a maternal factor essential for early development, plays a critical role in the regulation of DNA methylation, transcriptional repression, chromatin condensation, and cell division and the maintenance of cell pluripotentiality. Despite the fundamental roles of PGC7 in these cellular processes, only a few molecular and functional interactions of PGC7 have been reported. Here, a streptavidin-biotin affinity purification technique combined with LC-MS/MS was used to analyze potential proteins that interact with PGC7. In total, 291 potential PGC7-interacting proteins were identified. Through an in-depth bioinformatic analysis of potential interactors, we linked PGC7 to critical cellular processes including translation, RNA processing, cell cycle, and regulation of heterochromatin structure. To better understand the functional interactions of PGC7 with its potential interactors, we constructed a protein-protein interaction network using the STRING database. In addition, we discussed in detail the interactions between PGC7 and some of its newly validated partners. The identification of these potential interactors of PGC7 expands our knowledge on the PGC7 interactome and provides a valuable resource for understanding the diverse functions of this protein.

Keywords: LC−MS/MS; PGC7; RNA processing; cell cycle; heterochromatin structure; protein−protein interaction network; unfolded protein.

MeSH terms

  • Animals
  • Carbon-Nitrogen Ligases / genetics
  • Carbon-Nitrogen Ligases / metabolism
  • Cell Cycle / genetics
  • Chromatography, Liquid
  • Chromosomal Proteins, Non-Histone
  • Cloning, Molecular
  • DNA Methylation
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Gene Expression Regulation
  • Gene Regulatory Networks*
  • HEK293 Cells
  • Heterochromatin / chemistry
  • Heterochromatin / metabolism*
  • Humans
  • Mice
  • Molecular Sequence Annotation
  • Oligopeptides / genetics
  • Oligopeptides / metabolism
  • Plasmids / chemistry
  • Plasmids / metabolism
  • Protein Binding
  • Protein Biosynthesis
  • Protein Interaction Mapping*
  • Proteomics / methods*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Tandem Mass Spectrometry


  • Chromosomal Proteins, Non-Histone
  • Dppa3 protein, mouse
  • Escherichia coli Proteins
  • Heterochromatin
  • Oligopeptides
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • FLAG peptide
  • Carbon-Nitrogen Ligases
  • birA protein, E coli