Journal article
Transcriptional Regulation by Lge1p Requires a Function Independent of Its Role in Histone H2B Ubiquitination
The Journal of biological chemistry, Vol.280(4), pp.2759-2770
01/28/2005
DOI: 10.1074/jbc.M408333200
PMID: 15528187
Abstract
Saccharomyces cerevisiae cells that have lost their mitochondrial genome (ρ0) strongly induce transcription of multidrug resistance genes, including the ATP-binding cassette transporter gene PDR5. PDR5 induction in ρ0 cells requires the presence of the zinc cluster transcription factor Pdr3p. The PDR3 gene is positively autoregulated in ρ0 cells by virtue of the presence of two binding sites for Pdr3p in its promoter. We identify the novel protein Lge1p as a required participant in the ρ0 activation of PDR3 and PDR5 expression. Lge1p is a nuclear protein that has been found to play a role in ubiquitination of histone H2B at Lys123. This ubiquitination requires the presence of the ubiquitin-conjugating enzyme Rad6p and the ubiquitin ligase Bre1p. Interestingly, ρ0 strains lacking Lge1p failed to induce PDR3 transcription, but induction was still seen in Δrad6, Δbre1, and H2B-K123R mutant strains. Microarray experiments also confirmed that the pattern of gene expression changes seen in cells lacking Lge1p, Bre1p, or Rad6p or containing the H2B-K123R mutant as the only form of H2B share some overlap but are distinct. These findings provide a strong argument that Lge1p has roles in gene regulation independent of its participation in the Rad6p-dependent ubiquitination of H2B.
Details
- Title: Subtitle
- Transcriptional Regulation by Lge1p Requires a Function Independent of Its Role in Histone H2B Ubiquitination
- Creators
- Xiaoting Zhang - University of IowaAnia Kolaczkowska - University of IowaFrédéric Devaux - Laboratoire de Génétique Moléculaire, CNRS, Ecole Normale Supérieure, 75230 Paris, Cedex 05, FranceSneh Lata Panwar - University of IowaTimothy C. Hallstrom - University of IowaClaude Jacq - Laboratoire de Génétique Moléculaire, CNRS, Ecole Normale Supérieure, 75230 Paris, Cedex 05, FranceW. Scott Moye-Rowley - University of Iowa
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.280(4), pp.2759-2770
- DOI
- 10.1074/jbc.M408333200
- PMID
- 15528187
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 01/28/2005
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984297511002771
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