{"entity": "researcher", "timestamp": "2026-11-08T07:08:34.043Z", "family": "Carlstr\u00f6m", "given": "Andreas", "initials": "A", "orcid": "0000-0001-6159-8753", "affiliations": ["Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/862f5495c9144a5faf160701de688d35.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/862f5495c9144a5faf160701de688d35"}}, "publications": [{"entity": "publication", "iuid": "7a1f58b0bbb84172b4856301839cafee", "links": {"self": {"href": "https://publications.scilifelab.se/publication/7a1f58b0bbb84172b4856301839cafee.json"}, "display": {"href": "https://publications.scilifelab.se/publication/7a1f58b0bbb84172b4856301839cafee"}}, "title": "Mitochondrial respirasome-like supercomplexes support metabolic flexibility in yeast.", "authors": [{"family": "Eldeeb", "given": "Mazzen H", "initials": "MH", "orcid": "0000-0001-8724-5999", "researcher": {"href": "https://publications.scilifelab.se/researcher/1e39cc5bc0814db2b1d86652b8e42f85.json"}}, {"family": "Cosner", "given": "Zoe", "initials": "Z"}, {"family": "Carlstr\u00f6m", "given": "Andreas", "initials": "A", "orcid": "0000-0001-6159-8753", "researcher": {"href": "https://publications.scilifelab.se/researcher/862f5495c9144a5faf160701de688d35.json"}}, {"family": "Mays", "given": "Jeffri-Noelle", "initials": "JN"}, {"family": "Rodriguez", "given": "Gabriella F", "initials": "GF", "orcid": "0000-0002-1394-6191", "researcher": {"href": "https://publications.scilifelab.se/researcher/41d49841e2854cc6b2847685708784f5.json"}}, {"family": "Berndtsson", "given": "Jens", "initials": "J", "orcid": "0000-0001-6627-8134", "researcher": {"href": "https://publications.scilifelab.se/researcher/7620a5c7c0f245a28771d57d7179abbd.json"}}, {"family": "Ott", "given": "Martin", "initials": "M", "orcid": "0000-0001-6367-3091", "researcher": {"href": "https://publications.scilifelab.se/researcher/b27b582dbd2a47bcbb0fb3194277902a.json"}}, {"family": "Fontanesi", "given": "Flavia", "initials": "F", "orcid": "0000-0003-0509-3835", "researcher": {"href": "https://publications.scilifelab.se/researcher/b9e3a10c9beb46a09e4e3a22c08dfb4b.json"}}], "type": "journal article", "published": "2026-04-21", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "17", "issue": "1", "issn-l": "2041-1723"}, "abstract": "The mitochondrial respiratory chain (MRC) complexes, crucial for aerobic energy transduction in eukaryotes, form conserved higher-order structures called supercomplexes (SCs). The elucidation of SC physiological relevance is critical for our understanding of mitochondrial function and bioenergetics but has been hindered by the limited availability of experimental models isolating SC formation as the sole variable. In baker's yeast, SCs comprise III2IV1 and III2IV2 configurations, which enhance respiratory rates by facilitating cytochrome c diffusion along the SC surface. However, the roles of distinct SC conformations and MRC plasticity remain unclear. To address these questions, we engineered a yeast strain expressing a covalently-linked III2IV2 SC, structurally like the wild-type. Expression of this tethered SC supports robust respiratory activity but selectively impacts cytosolic NADH-driven respiration, due to distinct interactions with the NADH dehydrogenase Nde1. We propose that in yeast mitochondria, substrate-specific respirasome-like SCs contribute to the optimization of electron fluxes and support metabolic flexibility.", "doi": "10.1038/s41467-026-72228-8", "pmid": "42014734", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC13284296"}, {"db": "pii", "key": "10.1038/s41467-026-72228-8"}], "notes": [], "created": "2026-11-05T14:00:02.545Z", "modified": "2026-11-05T14:00:02.734Z"}, {"entity": "publication", "iuid": "691843567d344fc9a0cb6ef1ac44809e", "links": {"self": {"href": "https://publications.scilifelab.se/publication/691843567d344fc9a0cb6ef1ac44809e.json"}, "display": {"href": "https://publications.scilifelab.se/publication/691843567d344fc9a0cb6ef1ac44809e"}}, "title": "Translational activators align mRNAs at the small mitoribosomal subunit for translation initiation.", "authors": [{"family": "Bridgers", "given": "Joseph B", "initials": "JB"}, {"family": "Carlstr\u00f6m", "given": "Andreas", "initials": "A", "orcid": "0000-0001-6159-8753", "researcher": {"href": "https://publications.scilifelab.se/researcher/862f5495c9144a5faf160701de688d35.json"}}, {"family": "Sherpa", "given": "Dawafuti", "initials": "D"}, {"family": "Couvillion", "given": "Mary T", "initials": "MT"}, {"family": "Rov\u0161nik", "given": "Ur\u0161ka", "initials": "U", "orcid": "0000-0001-5889-6899", "researcher": {"href": "https://publications.scilifelab.se/researcher/199ce7dade164889902f7ae01e4b4577.json"}}, {"family": "Gao", "given": "Jingjing", "initials": "J"}, {"family": "Wan", "given": "Bowen", "initials": "B"}, {"family": "Shao", "given": "Sichen", "initials": "S", "orcid": "0000-0003-2679-5537", "researcher": {"href": "https://publications.scilifelab.se/researcher/e43a26465e7745cab4886422262a9bd0.json"}}, {"family": "Ott", "given": "Martin", "initials": "M", "orcid": "0000-0001-6367-3091", "researcher": {"href": "https://publications.scilifelab.se/researcher/b27b582dbd2a47bcbb0fb3194277902a.json"}}, {"family": "Churchman", "given": "L Stirling", "initials": "LS", "orcid": "0000-0003-3888-2574", "researcher": {"href": "https://publications.scilifelab.se/researcher/89e8493a62f34372a2315646df1ee73c.json"}}], "type": "journal article", "published": "2026-02-00", "journal": {"title": "Nat. Struct. Mol. Biol.", "issn": "1545-9985", "volume": "33", "issue": "2", "pages": "245-258", "issn-l": "1545-9985"}, "abstract": "Mitochondrial gene expression is essential for oxidative phosphorylation. Mitochondrial-encoded mRNAs are translated by dedicated mitochondrial ribosomes (mitoribosomes), whose regulation remains elusive. In Saccharomyces cerevisiae, nuclear-encoded mitochondrial translational activators (TAs) facilitate transcript-specific translation by a yet unknown mechanism. Here, we investigated the function of TAs containing RNA-binding pentatricopeptide repeats using selective mitoribosome profiling and cryo-electron microscopy (cryo-EM) structural analysis. These analyses show that TAs exhibit strong selectivity for mitoribosomes initiating on their target transcripts. Moreover, TA-mitoribosome footprints indicate that TAs recruit mitoribosomes proximal to the start codon. Two cryo-EM structures of mRNA-TA complexes bound to mitoribosomes stalled in the post-initiation, pre-elongation state revealed the general mechanism of TA action. Specifically, the TAs bind to structural elements in the 5' untranslated region of the client mRNA and the mRNA channel exit to align the mRNA in the small subunit during initiation. Our findings provide a mechanistic basis for understanding how mitochondria achieve transcript-specific translation initiation without relying on general sequence elements to position mitoribosomes at start codons.", "doi": "10.1038/s41594-025-01726-y", "pmid": "41339860", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC12916500"}, {"db": "pii", "key": "10.1038/s41594-025-01726-y"}], "notes": [], "created": "2026-11-05T14:06:32.194Z", "modified": "2026-11-05T14:06:32.309Z"}]}