Academic Journal

Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility.

التفاصيل البيبلوغرافية
العنوان: Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility.
المؤلفون: Wu, Hao, Muñoz, Elise, Hsieh, Laura, Gourdet, Muryam, Narlikar, Geeta, Cheng, Yifan, Chio, Un Seng
المصدر: Science, vol 381, iss 6655
بيانات النشر: eScholarship, University of California
سنة النشر: 2023
المجموعة: University of California: eScholarship
مصطلحات موضوعية: Chromatin, Chromatin Assembly and Disassembly, Histones, Nucleosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
الوصف: Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of Saccharomyces cerevisiae INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location -2 (SHL -2), in contrast to SHL -6 and SHL -7, as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes such that Ino80 is maximally active near SHL -2. The SHL -2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that subnucleosomal particles play considerable regulatory roles.
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: unknown
Relation: qt30q5d2xq; https://escholarship.org/uc/item/30q5d2xq
الاتاحة: https://escholarship.org/uc/item/30q5d2xq
Rights: public
رقم الانضمام: edsbas.7B279D43
قاعدة البيانات: BASE