Crystal structure of yeast Gid10 in complex with Pro/N-degron

Jin Seok Shin, Si Hoon Park, Leehyeon Kim, Jiwon Heo, Hyun Kyu Song

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

The cellular glucose level has to be tightly regulated by a variety of cellular processes. One of them is the degradation of gluconeogenic enzymes such as Fbp1, Icl1, Mdh2, and Pck1 by GID (glucose-induced degradation deficient) E3 ubiquitin ligase. The Gid4 component of the GID ligase complex is responsible for recognizing the N-terminal proline residue of the target substrates under normal conditions. However, an alternative N-recognin Gid10 controls the degradation process under stressed conditions. Although Gid10 shares a high sequence similarity with Gid4, their substrate specificities are quite different. Here, we report the structure of Gid10 from Saccharomyces cerevisiae in complex with Pro/N-degron, Pro-Tyr-Ile-Thr, which is almost identical to the sequence of the natural substrate Art2. Although Gid10 shares many structural features with the Gid4 protein from yeast and humans, the current structure explains the unique structural difference for the preference of bulky hydrophobic residue at the second position of Pro/N-degron. Therefore, this study provides a fundamental basis for understanding of the structural diversity and substrate specificity of recognition components in the GID E3 ligase complex involved in the Pro/N-degron pathway.

Original languageEnglish
Pages (from-to)86-92
Number of pages7
JournalBiochemical and biophysical research communications
Volume582
DOIs
Publication statusPublished - 2021 Dec 10

Keywords

  • E3 ubiquitin ligase
  • GID complex
  • N-degron
  • Proline
  • Saccharomyces cerevisiae
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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