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Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1статья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 21 августа 2017 г.
- Авторы: Lomakin Ivan B., Stolboushkina Elena A., Vaidya Anand T., Chenguang Zhao, Garber Maria B., Dmitriev Sergey E., Steitz Thomas A.
- Журнал: Cell reports
- Том: 20
- Номер: 3
- Год издания: 2017
- Издательство: Cell Press
- Местоположение издательства: United States
- Первая страница: 521
- Последняя страница: 528
- DOI: 10.1016/j.celrep.2017.06.025
- Аннотация: The repertoire of the density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein was recently expanded to include translational control of a specific set of cancer-related mRNAs. DENR and MCT-1 form the heterodimer, which binds to the ribosome and operates at both translation initiation and reinitiation steps, though by a mechanism that is yet unclear. Here, we determined the crystal structure of the human small ribosomal subunit in complex with DENR-MCT-1. The structure reveals the location of the DENR-MCT-1 dimer bound to the small ribosomal subunit. The binding site of the C-terminal domain of DENR on the ribosome has a striking similarity with those of canonical initiation factor 1 (eIF1), which controls the fidelity of translation initiation and scanning. Our findings elucidate how the DENR-MCT-1 dimer interacts with the ribosome and have functional implications for the mechanism of unconventional translation initiation and reinitiation.
- Добавил в систему: Дмитриев Сергей Евгеньевич