Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9736
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dc.contributor.authorBronkhorst, Alfred W.-
dc.contributor.authorLee, Chop Y.-
dc.contributor.authorMöckel, Martin M.-
dc.contributor.authorRuegenberg, Sabine-
dc.contributor.authorJesus Domingues, Antonio de-
dc.contributor.authorSadouki, Shéraz-
dc.contributor.authorPiccinno, Rossana-
dc.contributor.authorSumiyosh, Tetsutaro-
dc.contributor.authorSiomi, Mikiko C.-
dc.contributor.authorStelzl, Lukas-
dc.contributor.authorLuck, Katja-
dc.contributor.authorKetting, René F.-
dc.date.accessioned2023-12-11T09:56:29Z-
dc.date.available2023-12-11T09:56:29Z-
dc.date.issued2023-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/9754-
dc.description.abstractPiwi-interacting RNAs (piRNAs) direct PIWI proteins to transposons to silence them, thereby preserving genome integrity and fertility. The piRNA population can be expanded in the ping-pong amplification loop. Within this process, piRNA-associated PIWI proteins (piRISC) enter a membraneless organelle called nuage to cleave their target RNA, which is stimulated by Gtsf proteins. The resulting cleavage product gets loaded into an empty PIWI protein to form a new piRISC complex. However, for piRNA amplification to occur, the new RNA substrates, Gtsf-piRISC, and empty PIWI proteins have to be in physical proximity. In this study, we show that in silkworm cells, the Gtsf1 homolog BmGtsf1L binds to piRNA-loaded BmAgo3 and localizes to granules positive for BmAgo3 and BmVreteno. Biochemical assays further revealed that conserved residues within the unstructured tail of BmGtsf1L directly interact with BmVreteno. Using a combination of AlphaFold modeling, atomistic molecular dynamics simulations, and in vitro assays, we identified a novel binding interface on the BmVreteno-eTudor domain, which is required for BmGtsf1L binding. Our study reveals that a single eTudor domain within BmVreteno provides two binding interfaces and thereby interconnects piRNA-loaded BmAgo3 and BmGtsf1L.en_GB
dc.language.isoengde
dc.rightsCC BY*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleAn extended Tudor domain within Vreteno interconnects Gtsf1L and Ago3 for piRNA biogenesis in Bombyx morien_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-9736-
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 10 Biologiede
jgu.organisation.number7970-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleThe EMBO journalde
jgu.journal.volume42de
jgu.pages.alternativee114072de
jgu.publisher.year2023-
jgu.publisher.nameWileyde
jgu.publisher.placeHoboken, NJ u.a.de
jgu.publisher.issn0261-4189de
jgu.organisation.placeMainz-
jgu.subject.ddccode570de
jgu.publisher.doi10.15252/embj.2023114072de
jgu.organisation.rorhttps://ror.org/023b0x485-
jgu.subject.dfgLebenswissenschaftende
Appears in collections:DFG-491381577-H

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