The 19S complex of the proteasome regulates nucleotide excision repair in yeast

Thomas G. Gillette, Wenya Huang, Steven Jon Russell, Simon H. Reed, Stephen Albert Johnston, Errol C. Friedberg

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

Previous studies suggest that the amino-terminal ubiquitin-like (ubl) domain of Rad23 protein can recruit the proteasome for a stimulatory role during nucleotide excision repair in the yeast Saccharomyces cerevisiae. In this report, we show that the 19S regulatory complex of the yeast proteasome can affect nucleotide excision repair independently of Rad23 protein. Strains with mutations in 19S regulatory subunits (but not 20S subunits) of the proteasome promote partial recovery of nucleotide excision repair in vivo in rad23 deletion mutants, but not in other nucleotide excision repair-defective strains tested. In addition, a strain that expresses a temperature-degradable ATPase subunit of the 19S regulatory complex manifests a dramatically increased rate of nucleotide excision repair in vivo. These data indicate that the 19S regulatory complex of the 26S proteasome can negatively regulate the rate of nucleotide excision repair in yeast and suggest that Rad23 protein not only recruits the 19S regulatory complex, but also can mediate functional interactions between the 19S regulatory complex and the nucleotide excision repair machinery. The 19S regulatory complex of the yeast proteasome functions in nucleotide excision repair independent of proteolysis.

Original languageEnglish (US)
Pages (from-to)1528-1539
Number of pages12
JournalGenes and Development
Volume15
Issue number12
DOIs
StatePublished - Jun 15 2001

Fingerprint

Proteasome Endopeptidase Complex
DNA Repair
Yeasts
Ubiquitin
Proteolysis
Saccharomyces cerevisiae
Adenosine Triphosphatases
Proteins
Mutation
Temperature

Keywords

  • DNA repair
  • Proteasome
  • Rad23 protein
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

Cite this

Gillette, T. G., Huang, W., Russell, S. J., Reed, S. H., Johnston, S. A., & Friedberg, E. C. (2001). The 19S complex of the proteasome regulates nucleotide excision repair in yeast. Genes and Development, 15(12), 1528-1539. https://doi.org/10.1101/gad.869601

The 19S complex of the proteasome regulates nucleotide excision repair in yeast. / Gillette, Thomas G.; Huang, Wenya; Russell, Steven Jon; Reed, Simon H.; Johnston, Stephen Albert; Friedberg, Errol C.

In: Genes and Development, Vol. 15, No. 12, 15.06.2001, p. 1528-1539.

Research output: Contribution to journalArticle

Gillette, TG, Huang, W, Russell, SJ, Reed, SH, Johnston, SA & Friedberg, EC 2001, 'The 19S complex of the proteasome regulates nucleotide excision repair in yeast', Genes and Development, vol. 15, no. 12, pp. 1528-1539. https://doi.org/10.1101/gad.869601
Gillette, Thomas G. ; Huang, Wenya ; Russell, Steven Jon ; Reed, Simon H. ; Johnston, Stephen Albert ; Friedberg, Errol C. / The 19S complex of the proteasome regulates nucleotide excision repair in yeast. In: Genes and Development. 2001 ; Vol. 15, No. 12. pp. 1528-1539.
@article{e10b8806e5dc44c69d0db179005f7b7e,
title = "The 19S complex of the proteasome regulates nucleotide excision repair in yeast",
abstract = "Previous studies suggest that the amino-terminal ubiquitin-like (ubl) domain of Rad23 protein can recruit the proteasome for a stimulatory role during nucleotide excision repair in the yeast Saccharomyces cerevisiae. In this report, we show that the 19S regulatory complex of the yeast proteasome can affect nucleotide excision repair independently of Rad23 protein. Strains with mutations in 19S regulatory subunits (but not 20S subunits) of the proteasome promote partial recovery of nucleotide excision repair in vivo in rad23 deletion mutants, but not in other nucleotide excision repair-defective strains tested. In addition, a strain that expresses a temperature-degradable ATPase subunit of the 19S regulatory complex manifests a dramatically increased rate of nucleotide excision repair in vivo. These data indicate that the 19S regulatory complex of the 26S proteasome can negatively regulate the rate of nucleotide excision repair in yeast and suggest that Rad23 protein not only recruits the 19S regulatory complex, but also can mediate functional interactions between the 19S regulatory complex and the nucleotide excision repair machinery. The 19S regulatory complex of the yeast proteasome functions in nucleotide excision repair independent of proteolysis.",
keywords = "DNA repair, Proteasome, Rad23 protein, Saccharomyces cerevisiae",
author = "Gillette, {Thomas G.} and Wenya Huang and Russell, {Steven Jon} and Reed, {Simon H.} and Johnston, {Stephen Albert} and Friedberg, {Errol C.}",
year = "2001",
month = "6",
day = "15",
doi = "10.1101/gad.869601",
language = "English (US)",
volume = "15",
pages = "1528--1539",
journal = "Genes and Development",
issn = "0890-9369",
publisher = "Cold Spring Harbor Laboratory Press",
number = "12",

}

TY - JOUR

T1 - The 19S complex of the proteasome regulates nucleotide excision repair in yeast

AU - Gillette, Thomas G.

AU - Huang, Wenya

AU - Russell, Steven Jon

AU - Reed, Simon H.

AU - Johnston, Stephen Albert

AU - Friedberg, Errol C.

PY - 2001/6/15

Y1 - 2001/6/15

N2 - Previous studies suggest that the amino-terminal ubiquitin-like (ubl) domain of Rad23 protein can recruit the proteasome for a stimulatory role during nucleotide excision repair in the yeast Saccharomyces cerevisiae. In this report, we show that the 19S regulatory complex of the yeast proteasome can affect nucleotide excision repair independently of Rad23 protein. Strains with mutations in 19S regulatory subunits (but not 20S subunits) of the proteasome promote partial recovery of nucleotide excision repair in vivo in rad23 deletion mutants, but not in other nucleotide excision repair-defective strains tested. In addition, a strain that expresses a temperature-degradable ATPase subunit of the 19S regulatory complex manifests a dramatically increased rate of nucleotide excision repair in vivo. These data indicate that the 19S regulatory complex of the 26S proteasome can negatively regulate the rate of nucleotide excision repair in yeast and suggest that Rad23 protein not only recruits the 19S regulatory complex, but also can mediate functional interactions between the 19S regulatory complex and the nucleotide excision repair machinery. The 19S regulatory complex of the yeast proteasome functions in nucleotide excision repair independent of proteolysis.

AB - Previous studies suggest that the amino-terminal ubiquitin-like (ubl) domain of Rad23 protein can recruit the proteasome for a stimulatory role during nucleotide excision repair in the yeast Saccharomyces cerevisiae. In this report, we show that the 19S regulatory complex of the yeast proteasome can affect nucleotide excision repair independently of Rad23 protein. Strains with mutations in 19S regulatory subunits (but not 20S subunits) of the proteasome promote partial recovery of nucleotide excision repair in vivo in rad23 deletion mutants, but not in other nucleotide excision repair-defective strains tested. In addition, a strain that expresses a temperature-degradable ATPase subunit of the 19S regulatory complex manifests a dramatically increased rate of nucleotide excision repair in vivo. These data indicate that the 19S regulatory complex of the 26S proteasome can negatively regulate the rate of nucleotide excision repair in yeast and suggest that Rad23 protein not only recruits the 19S regulatory complex, but also can mediate functional interactions between the 19S regulatory complex and the nucleotide excision repair machinery. The 19S regulatory complex of the yeast proteasome functions in nucleotide excision repair independent of proteolysis.

KW - DNA repair

KW - Proteasome

KW - Rad23 protein

KW - Saccharomyces cerevisiae

UR - http://www.scopus.com/inward/record.url?scp=0035876040&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035876040&partnerID=8YFLogxK

U2 - 10.1101/gad.869601

DO - 10.1101/gad.869601

M3 - Article

VL - 15

SP - 1528

EP - 1539

JO - Genes and Development

JF - Genes and Development

SN - 0890-9369

IS - 12

ER -