STI1 domain dynamically engages transient helices in disordered regions to drive self-association and phase separation of yeast ubiquilin Dsk2.

• Tác giả: Nirbhik Acharya, Carlos A Castañeda, Emily A Daniel, Thuy P Dao, Daniel A Kraut, Erin Mulvey, Jessica K Niblo, Jeroen Roelofs, Shahar Sukenik
• Ngôn ngữ: eng
• Ký hiệu phân loại: 133.594 Types or schools of astrology originating in or associated with a
• Thông tin xuất bản: United States : bioRxiv : the preprint server for biology , 2025
• Bộ sưu tập: NCBI
• ID: 742430

Tóm tắt

UNLABELLED: Ubiquitin-binding shuttle proteins are important components of stress-induced biomolecular condensates in cells. Yeast Dsk2 scaffolds proteasome-containing condensates via multivalent interactions with proteasomes and ubiquitinated substrates under azide-induced mitochondrial stress or extended growth conditions. However, the molecular mechanisms underlying how these shuttle proteins work are unknown. Here, we identify that the middle chaperone-binding STI1 domain is the main driver of Dsk2 self-association and phase separation HIGHLIGHTS: The intrinsically disordered regions of Dsk2 harbor transient helices that regulate protein properties via interactions with the STI1 domain. The STI1 domain is a significant driver of Dsk2 self-association and phase separation