ArticleJournal of molecular biology2013
Unfolding of the C-terminal domain of the J-protein Zuo1 releases autoinhibition and activates Pdr1-dependent transcription.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- The Zuo1 C-terminal domain stabilizes DNA guanosine quadruplex (G4) structures located on Chromosome IX in Saccharomyces cerevisiae.Nucleic acids research · 2025Article
- InAIMS microbiology · 2025Article
- Structural characterization of the ACDC domain from ApiAP2 proteins, a potential molecular target against apicomplexan parasites.Acta crystallographica. Section D, Structural biology · 2025Article
- Activity of the pleiotropic drug resistance transcription factors Pdr1p and Pdr3p is modulated by binding site flanking sequences.FEBS letters · 2024Article
- Moonlighting Proteins: Diverse Functions Found in Fungi.Journal of fungi (Basel, Switzerland) · 2023Review
- Structural inventory of cotranslational protein folding by the eukaryotic RAC complex.Nature structural & molecular biology · 2023Article
- Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control.Cell reports · 2022Article
- Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.Nature communications · 2022Article
- J-like protein family of Arabidopsis thaliana: the enigmatic cousins of J-domain proteins.Plant cell reports · 2022Review
- The Relevance of G-Quadruplexes for DNA Repair.International journal of molecular sciences · 2021Review
- Deciphering molecular details of the RAC-ribosome interaction by EPR spectroscopy.Scientific reports · 2021Article
- Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair.Nature communications · 2020Article
- The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb.Nature communications · 2020Article
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- Multiple interfaces control activity of the Candida glabrata Pdr1 transcription factor mediating azole drug resistance.Current genetics · 2019Review
- Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70.PloS one · 2019Article
- Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC.Nature structural & molecular biology · 2017Review
- How Do J-Proteins Get Hsp70 to Do So Many Different Things?Trends in biochemical sciences · 2017Review
- Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.Nature structural & molecular biology · 2016Article
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6 authors at 2 institutions in 1 country.
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Abstract
The C-terminal 69 residues of the J-protein Zuo1 are sufficient to activate Pdr1, a transcription factor involved in both pleiotropic drug resistance and growth control. Little is understood about the pathway of activation by this primarily ribosome associated Hsp40 co-chaperone. Here, we report that only the C-terminal 13 residues of Zuo1 are required for activation of Pdr1, with hydrophobic residues being critical for activity. Two-hybrid interaction experiments suggest that the interaction between this 13-residue Zuo1 peptide and Pdr1 is direct, analogous to the activation of Pdr1 by xenobiotics. However, simply dissociation of Zuo1 from the ribosome is not sufficient for induction of Pdr1 transcriptional activity, as the C-terminal 86 residues of Zuo1 fold into an autoinhibitory left-handed four-helix bundle. Hydrophobic residues critical for interaction with Pdr1 are sequestered within the structure of this C-terminal domain (CTD), necessitating unfolding for activation. Thus, although expression of the CTD does not result in activation, alterations that destabilize the structure cause induction of pleiotropic drug resistance. These destabilizing alterations also result in dissociation of the full-length protein from the ribosome. Thus, our results are consistent with an activation pathway in which unfolding of Zuo1's C-terminal helical bundle domain results in ribosome dissociation followed by activation of Pdr1 via a direct interaction.
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