دورية أكاديمية

Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance.

التفاصيل البيبلوغرافية
العنوان: Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance.
المؤلفون: Prasanna Satpute-Krishnan, Sara X Langseth, Tricia R Serio
المصدر: PLoS Biology, Vol 5, Iss 2, p e24 (2007)
بيانات النشر: Public Library of Science (PLoS), 2007.
سنة النشر: 2007
المجموعة: LCC:Biology (General)
مصطلحات موضوعية: Biology (General), QH301-705.5
الوصف: Inheritance of phenotypic traits depends on two key events: replication of the determinant of that trait and partitioning of these copies between mother and daughter cells. Although these processes are well understood for nucleic acid-based genes, the mechanisms by which protein-only or prion-based genetic elements direct phenotypic inheritance are poorly understood. Here, we report a process crucial for inheritance of the Saccharomyces cerevisiae prion [PSI(+)], a self-replicating conformer of the Sup35 protein. By tightly controlling expression of a Sup35-GFP fusion, we directly observe remodeling of existing Sup35([PSI+]) complexes in vivo. This dynamic change in Sup35([PSI+]) is lost when the molecular chaperone Hsp104, a factor essential for propagation of all yeast prions, is functionally impaired. The loss of Sup35([PSI+]) remodeling by Hsp104 decreases the mobility of these complexes in the cytosol, creates a segregation bias that limits their transmission to daughter cells, and consequently diminishes the efficiency of conversion of newly made Sup35 to the prion form. Our observations resolve several seemingly conflicting reports on the mechanism of Hsp104 action and point to a single Hsp104-dependent event in prion propagation.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1544-9173
1545-7885
Relation: http://europepmc.org/articles/PMC1779812?pdf=render; https://doaj.org/toc/1544-9173; https://doaj.org/toc/1545-7885
DOI: 10.1371/journal.pbio.0050024
URL الوصول: https://doaj.org/article/5ffa27cd19b64bdda752a8c08d3599d1
رقم الأكسشن: edsdoj.5ffa27cd19b64bdda752a8c08d3599d1
قاعدة البيانات: Directory of Open Access Journals