دورية أكاديمية

Complete subunit architecture of the proteasome regulatory particle

التفاصيل البيبلوغرافية
العنوان: Complete subunit architecture of the proteasome regulatory particle
المؤلفون: Lander, Gabriel C, Estrin, Eric, Matyskiela, Mary E, Bashore, Charlene, Nogales, Eva, Martin, Andreas
المصدر: Nature, vol 482, iss 7384
بيانات النشر: eScholarship, University of California
سنة النشر: 2012
المجموعة: University of California: eScholarship
مصطلحات موضوعية: Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Adenosine Triphosphatases, Adenosine Triphosphate, Binding Sites, Endopeptidases, Escherichia coli, Holoenzymes, Models, Molecular, Proteasome Endopeptidase Complex, Protein Binding, Protein Conformation, Protein Subunits, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin, General Science & Technology
جغرافية الموضوع: 186 - 191
الوصف: The proteasome is the major ATP-dependent protease in eukaryotic cells, but limited structural information restricts a mechanistic understanding of its activities. The proteasome regulatory particle, consisting of the lid and base subcomplexes, recognizes and processes polyubiquitinated substrates. Here we used electron microscopy and a new heterologous expression system for the lid to delineate the complete subunit architecture of the regulatory particle from yeast. Our studies reveal the spatial arrangement of ubiquitin receptors, deubiquitinating enzymes and the protein unfolding machinery at subnanometre resolution, outlining the substrate's path to degradation. Unexpectedly, the ATPase subunits within the base unfoldase are arranged in a spiral staircase, providing insight into potential mechanisms for substrate translocation through the central pore. Large conformational rearrangements of the lid upon holoenzyme formation suggest allosteric regulation of deubiquitination. We provide a structural basis for the ability of the proteasome to degrade a diverse set of substrates and thus regulate vital cellular processes.
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: unknown
العلاقة: qt9n59k8db; https://escholarship.org/uc/item/9n59k8dbTest
الإتاحة: https://escholarship.org/uc/item/9n59k8dbTest
حقوق: public
رقم الانضمام: edsbas.FF093F19
قاعدة البيانات: BASE