Journal
CELL REPORTS
Volume 20, Issue 3, Pages 521-528Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2017.06.025
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [P01 GM022778] Funding Source: Medline
- Russian Science Foundation [14-50-00060] Funding Source: Russian Science Foundation
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The repertoire of the density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT1/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.
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