1H, 13C and 15N assignments of Sgt2 N-terminal dimerisation domain and its binding partner, Get5 Ubiquitin-like domain

Aline C Simon, Peter J Simpson, William Hawthorne, Lisa R Hale, Rachael M Goldstone, Rivka L Isaacson

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

The first stage of the GET (guided entry of tail-anchored proteins) mechanism for tail-anchored (TA) membrane protein insertion is thought to occur when Sgt2 (small, glutamine-rich, tetratricopeptide repeat-containing protein 2) binds TA proteins upon their release from the ribosome. It sorts them and passes the majority over to a complex of Get5 and Get4 for transmission along the GET pathway and delivery to their membrane destination. Sgt2 is a 38 kDa protein consisting of three domains. The N-terminal domain effects tight dimerisation of the protein and is also the site for binding with the ubiquitin-like (UBL) domain of Get5. Here we have expressed and purified uniformly-(15)N/(13)C-labelled N-terminal Sgt2 (Sgt2_NT) and its binding partner, Get5 UBL domain (Get5_UBL) and assigned the backbone and side-chain resonances as a basis for structure solution of the individual components and, ultimately, the complex. This will provide detailed molecular insight into the early stages of the GET pathway.

Original languageEnglish
Pages (from-to)271-4
Number of pages4
JournalBiomolecular NMR Assignments
Volume7
Issue number2
DOIs
Publication statusPublished - Oct 2013

Keywords

  • Amino Acid Sequence
  • Carbon Isotopes
  • Carrier Proteins
  • Molecular Sequence Data
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Protons
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin

Fingerprint

Dive into the research topics of '1H, 13C and 15N assignments of Sgt2 N-terminal dimerisation domain and its binding partner, Get5 Ubiquitin-like domain'. Together they form a unique fingerprint.

Cite this