صورة
Image1_Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function.pdf
| العنوان: | Image1_Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function.pdf |
|---|---|
| المؤلفون: | Samantha J. Ganser, Bridget A. McNish, Gillian L. Schwanitz, John L. Delaney, Bridget A. Corpus, Brenda A. Schilke, Anup K. Biswal, Chandan Sahi, Elizabeth A. Craig, Justin K. Hines |
| سنة النشر: | 2024 |
| المجموعة: | Frontiers: Figshare |
| مصطلحات موضوعية: | Biochemistry, Molecular Biology, Structural Biology, Enzymes, Protein Trafficking, Proteomics and Intermolecular Interactions (excl. Medical Proteomics), Receptors and Membrane Biology, Signal Transduction, Structural Biology (incl. Macromolecular Modelling), Synthetic Biology, chaperone, amyloid, Hsp104, Hsp40, J-protein |
| الوصف: | J-domain proteins (JDPs) are obligate cochaperones of Hsp70s. The Class A JDP Apj1 of the yeast cytosol has an unusually complex region between the N-terminal J-domain and the substrate binding region—often called the G rich or GF region in Class A and B JDPs because of its typical abundance of glycine. The N-terminal 161-residue Apj1 fragment is known to be sufficient for Apj1 function in prion curing, driven by the overexpression of Hsp104. Further analyzing the N-terminal segment of Apj1, we found that a 90-residue fragment that includes the 70-residue J-domain and the adjacent 12-residue glutamine/alanine (Q/A) segment is sufficient for curing. Furthermore, the 121-residue fragment that includes the G rich region was sufficient to not only sustain the growth of cells lacking the essential Class B JDP Sis1 but also enabled the maintenance of several prions normally dependent on Sis1 for propagation. A J-domain from another cytosolic JDP could substitute for the Sis1-related functions but not for Apj1 in prion curing. Together, these results separate the functions of JDPs in prion biology and underscore the diverse functionality of multi-domain cytosolic JDPs in yeast. |
| نوع الوثيقة: | still image |
| اللغة: | unknown |
| العلاقة: | https://figshare.com/articles/figure/Image1_Unique_characteristics_of_the_J-domain_proximal_regions_of_Hsp70_cochaperone_Apj1_in_prion_propagation_elimination_and_its_overlap_with_Sis1_function_pdf/25681689Test |
| DOI: | 10.3389/fmolb.2024.1392608.s002 |
| الإتاحة: | https://doi.org/10.3389/fmolb.2024.1392608.s002Test https://figshare.com/articles/figure/Image1_Unique_characteristics_of_the_J-domain_proximal_regions_of_Hsp70_cochaperone_Apj1_in_prion_propagation_elimination_and_its_overlap_with_Sis1_function_pdf/25681689Test |
| حقوق: | CC BY 4.0 |
| رقم الانضمام: | edsbas.C110B477 |
| قاعدة البيانات: | BASE |
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