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Scientific article
English

Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination

Contributors

Panasenko, Olesya; David, Fabrice P A.; Collart, Martine

Published in

Genetics, vol. 181, no. 2, p. 447-460

Publication date

2009

Abstract

In this work we addressed the role of ubiquitination in the function of the nascent polypeptide-associated complex (NAC), named EGD in the yeast Saccharomyces cerevisiae. To this end, we first identified the lysines residues required for ubiquitination of EGD/NAC. While simultaneous mutation of many lysines in the alpha-subunit of NAC (Egd2p) was required to abolish its ubiquitination, for the beta-subunit of NAC (Egd1p), mutation of K29 and K30 was sufficient. We determined that the ubiquitination of the two EGD subunits was coordinated, occurring during growth first on Egd1p and then on Egd2p. Egd2p was ubiquitinated earlier during growth if Egd1p could not be ubiquitinated. The use of mutants revealed the importance of EGD ubiqutination for its ribosome association and stability. Finally, our study demonstrated an interaction of EGD/NAC with the proteasome and revealed the importance of the Not4p E3 ligase, responsible for EGD/NAC ubiquitination, in this association.

Keywords

  • Amino Acid Sequence
  • DNA-Binding Proteins/chemistry/genetics/metabolism
  • Dimerization
  • Genes, Fungal
  • Models, Molecular
  • Molecular Chaperones/chemistry/genetics/metabolism
  • Molecular Sequence Data
  • Multiprotein Complexes
  • Proteasome Endopeptidase Complex/metabolism
  • Protein Interaction Domains and Motifs
  • Protein Subunits
  • Ribosomal Proteins/genetics/metabolism
  • Ribosomes/metabolism
  • Saccharomyces cerevisiae/genetics/metabolism
  • Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism
  • Sequence Homology, Amino Acid
  • Transcription Factors/chemistry/genetics/metabolism
  • Ubiquitin-Conjugating Enzymes/genetics/metabolism
  • Ubiquitin-Protein Ligases/genetics/metabolism
  • Ubiquitination

UNIGE affiliation entities

UNIGE research groups

Citation (ISO format)

PANASENKO, Olesya, DAVID, Fabrice P A., COLLART, Martine. Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination. In: Genetics, 2009, vol. 181, n° 2, p. 447–460. doi: 10.1534/genetics.108.095422

Main files (1)

Article (Published version)

Secondary files (1)

Supplemental data

Identifiers

Additional URL for this publication

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2644939/?tool=pubmed

Journal ISSN

0016-6731
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Technical informations

Creation

02/03/2010 16:32:00

First validation

02/03/2010 16:32:00

Update

30/03/2023 09:42:13

Status update

30/03/2023 09:42:12

Last indexation

29/10/2024 13:03:13
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