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The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity

التفاصيل البيبلوغرافية
العنوان: The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity
المؤلفون: Mohammed Jamshad, Timothy J Knowles, Scott A White, Douglas G Ward, Fiyaz Mohammed, Kazi Fahmida Rahman, Max Wynne, Gareth W Hughes, Günter Kramer, Bernd Bukau, Damon Huber
المصدر: eLife, Vol 8 (2019)
بيانات النشر: eLife Sciences Publications Ltd, 2019.
سنة النشر: 2019
المجموعة: LCC:Medicine
LCC:Science
LCC:Biology (General)
مصطلحات موضوعية: SecA, ribosome, protein translocation, protein secretion, metal-binding domain, SAXS, Medicine, Science, Biology (General), QH301-705.5
الوصف: In bacteria, the translocation of proteins across the cytoplasmic membrane by the Sec machinery requires the ATPase SecA. SecA binds ribosomes and recognises nascent substrate proteins, but the molecular mechanism of nascent substrate recognition is unknown. We investigated the role of the C-terminal tail (CTT) of SecA in nascent polypeptide recognition. The CTT consists of a flexible linker (FLD) and a small metal-binding domain (MBD). Phylogenetic analysis and ribosome binding experiments indicated that the MBD interacts with 70S ribosomes. Disruption of the MBD only or the entire CTT had opposing effects on ribosome binding, substrate-protein binding, ATPase activity and in vivo function, suggesting that the CTT influences the conformation of SecA. Site-specific crosslinking indicated that F399 in SecA contacts ribosomal protein uL29, and binding to nascent chains disrupts this interaction. Structural studies provided insight into the CTT-mediated conformational changes in SecA. Our results suggest a mechanism for nascent substrate protein recognition.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2050-084X
Relation: https://elifesciences.org/articles/48385; https://doaj.org/toc/2050-084X
DOI: 10.7554/eLife.48385
URL الوصول: https://doaj.org/article/03c1fc4e168e4c638fbfaa1f143e7620
رقم الأكسشن: edsdoj.03c1fc4e168e4c638fbfaa1f143e7620
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2050084X
DOI:10.7554/eLife.48385