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Mechanism of membrane-tethered mitochondrial protein synthesis

DOI: 10.1126/science.abe0763 DOI Help

Authors: Yuzuru Itoh (Stockholm University; Karolinska Institutet) , Juni Andrell (Stockholm University; Karolinska Institutet) , Austin Choi (University of Miami Miller School of Medicine) , Uwe Richter (University of Helsinki; Newcastle University) , Priyanka Maiti (University of Miami Miller School of Medicine) , Robert B. Best (National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health) , Antoni Barrientos (University of Miami Miller School of Medicine) , Brendan J. Battersby (University of Helsinki) , Alexey Amunts (Stockholm University; Karolinska Institutet)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Science , VOL 371 , PAGES 846 - 849

State: Published (Approved)
Published: February 2021
Diamond Proposal Number(s): 19823

Abstract: Mitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo–electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1–like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery.

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond

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