Lysine methylation modulates the protein-protein interactions of yeast cytochrome C Cyc1p

Daniel L. Winter, Dhanushi Abeygunawardena, Gene Hart-Smith, Melissa A. Erce, Marc R. Wilkins*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


In recent years, protein methylation has been established as a major intracellular PTM. It has also been proposed to modulate protein-protein interactions (PPIs) in the interactome. To investigate the effect of PTMs on PPIs, we recently developed the conditional two-hybrid (C2H) system. With this, we demonstrated that arginine methylation can modulate PPIs in the yeast interactome. Here, we used the C2H system to investigate the effect of lysine methylation. Specifically, we asked whether Ctm1p-mediated trimethylation of yeast cytochrome c Cyc1p, on lysine 78, modulates its interactions with Erv1p, Ccp1p, Cyc2p and Cyc3p. We show that the interactions between Cyc1p and Erv1p, and between Cyc1p and Cyc3p, are significantly increased upon trimethylation of lysine 78. This increase of interaction helps explain the reported facilitation of Cyc1p import into the mitochondrial intermembrane space upon methylation. This first application of the C2H system to the study of methyllysine-modulated interactions further confirms its robustness and flexibility.

Original languageEnglish
Pages (from-to)2166-2176
Number of pages11
Issue number13
Publication statusPublished - Jul 2015
Externally publishedYes


  • cytochrome c
  • lysine methylation
  • protein-protein interactions
  • systems biology
  • two-hybrid


Dive into the research topics of 'Lysine methylation modulates the protein-protein interactions of yeast cytochrome C Cyc1p'. Together they form a unique fingerprint.

Cite this