The Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly
Israel
Citation
Journal: Nat Commun / Year: 2026 Title: A small nucleolar RNA dictates the structure and function of translating ribosomes in Leishmania. Authors: K Shanmugha Rajan / Saurav Aryal / Sharanya Murugeshan / Yinzhou Zhu / Anat Bashan / Mika Olami / Hava Madmoni / Yuko Nobe / Tirza Doniger / Smadar Cohen-Chalamish / Eric Prina / Pascale ...Authors: K Shanmugha Rajan / Saurav Aryal / Sharanya Murugeshan / Yinzhou Zhu / Anat Bashan / Mika Olami / Hava Madmoni / Yuko Nobe / Tirza Doniger / Smadar Cohen-Chalamish / Eric Prina / Pascale Pescher / Tom Beneke / Masato Taoka / Christopher L Holley / Ron Unger / Gerald F Späth / Ada Yonath / Shulamit Michaeli / Abstract: The most common rRNA modification is 2'-O-methylation. Here, we determine the landscape of 2'-O-methylation in Leishmania, a parasite that cycles between two different hosts, insect and mammalian. We ...The most common rRNA modification is 2'-O-methylation. Here, we determine the landscape of 2'-O-methylation in Leishmania, a parasite that cycles between two different hosts, insect and mammalian. We find two 2'-O-methylated positions that are differentially modified during the parasite's two life stages. The deposition of these modifications is guided by snoRNAs. When we perform cytosine base-editing of the snoRNA responsible for guiding one of the two stage-regulated modifications, Am479, we fail to detect ribosomes lacking this modification, suggesting that it is essential. To better understand the role of the snoRNA and its guided modification, we determine the cryo-EM structures of ribosomes from cells overexpressing the guiding snoRNA and compare them to ribosomes from the parental strain. We do not find structural changes around Am479 or in the small subunit rRNA, but observe a difference in H68 of the large subunit rRNA due to a second base-pairing interaction, suggesting a potential chaperone activity for the snoRNA. Based on these results, translatome and tRNA analysis, we propose a mechanism whereby changes in ribosome structure affect the release of specific tRNAs, which correlate with changes in translation of only a subset of mRNAs.
Entire : CLASS-6_APE_CRYO-EM CONSENSUS MAP OF LD32CS1C1 EDITED RIBOSOMES I...
Entire
Name: CLASS-6_APE_CRYO-EM CONSENSUS MAP OF LD32CS1C1 EDITED RIBOSOMES IN COMPLEX WITH MRNA AND TRNA
Components
Complex: CLASS-6_APE_CRYO-EM CONSENSUS MAP OF LD32CS1C1 EDITED RIBOSOMES IN COMPLEX WITH MRNA AND TRNA
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Supramolecule #1: CLASS-6_APE_CRYO-EM CONSENSUS MAP OF LD32CS1C1 EDITED RIBOSOMES I...
Supramolecule
Name: CLASS-6_APE_CRYO-EM CONSENSUS MAP OF LD32CS1C1 EDITED RIBOSOMES IN COMPLEX WITH MRNA AND TRNA type: complex / ID: 1 / Parent: 0 Details: CLASS-6_APE_CRYO-EM CONSENSUS MAP OF LD32CS1C1 EDITED RIBOSOMES IN COMPLEX WITH MRNA AND TRNA
Source (natural)
Organism: Leishmania donovani (eukaryote)
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Experimental details
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Structure determination
Method
cryo EM
Processing
single particle reconstruction
Aggregation state
particle
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Sample preparation
Buffer
pH: 7.6
Vitrification
Cryogen name: ETHANE
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Electron microscopy
Microscope
TFS KRIOS
Image recording
Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 0.929 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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