Direct recognition of the C-terminal polylysine residues of nonstop protein by Ltn1, an E3 ubiquitin ligase

Kwang Hoon Sung, Hyun Kyu Song

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

When mRNAs lack stop codons, errors in gene expression and coding of aberrant proteins that are harmful in cells can result. In Saccharomyces cerevisiae, a 180-kDa E3-ubiquitin ligase, Ltn1 has been known to associate with ribosomes and marks translationally-arrested aberrant nascent polypeptides for proteasomal degradation. Here, we demonstrate the Ltn1 E3-ubiquitin ligase directly binds to the nonstop proteins and efficiently ubiquitylates them. The middle domain of Ltn1 is responsible for recognizing the polylysine residues of the nonstop protein with an affinity of 2-3 μM. This biochemical characterization of Ltn1 expands our knowledge regarding the fundamental process that removes aberrant nascent polypeptides in eukaryotes.

Original languageEnglish
Pages (from-to)642-647
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume453
Issue number3
DOIs
Publication statusPublished - 2014 Oct 24

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Polylysine
Ubiquitin-Protein Ligases
Peptides
Proteins
Terminator Codon
Eukaryota
Ribosomes
Gene expression
Yeast
Saccharomyces cerevisiae
Gene Expression
Degradation
Messenger RNA

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Direct recognition of the C-terminal polylysine residues of nonstop protein by Ltn1, an E3 ubiquitin ligase. / Sung, Kwang Hoon; Song, Hyun Kyu.

In: Biochemical and Biophysical Research Communications, Vol. 453, No. 3, 24.10.2014, p. 642-647.

Research output: Contribution to journalArticle

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