The Caenorhabditis elegans TDRD5/7-like protein, LOTR-1, interacts with the helicase ZNFX-1 to balance epigenetic signals in the germline.

Autor: Marnik EA; The MDI Biological Laboratory, Bar Harbor, Maine, United States of America.; Husson University, Bangor, Maine, United States of America., Almeida MV; Institute of Molecular Biology, Mainz, Germany.; International PhD Programme on Gene Regulation, Epigenetics & Genome Stability, Mainz, Germany., Cipriani PG; Center for Genomics & Systems Biology, New York University, New York, New York, United States of America.; Center for Genomics & Systems Biology, New York University Abu Dhabi, Abu Dhabi, United Arab Emirates., Chung G; Center for Genomics & Systems Biology, New York University, New York, New York, United States of America., Caspani E; Institute of Molecular Biology, Mainz, Germany.; International PhD Programme on Gene Regulation, Epigenetics & Genome Stability, Mainz, Germany., Karaulanov E; Institute of Molecular Biology, Mainz, Germany., Gan HH; Center for Genomics & Systems Biology, New York University, New York, New York, United States of America., Zinno J; Center for Genomics & Systems Biology, New York University, New York, New York, United States of America., Isolehto IJ; Institute of Molecular Biology, Mainz, Germany.; International PhD Programme on Gene Regulation, Epigenetics & Genome Stability, Mainz, Germany., Kielisch F; Institute of Molecular Biology, Mainz, Germany., Butter F; Institute of Molecular Biology, Mainz, Germany., Sharp CS; The MDI Biological Laboratory, Bar Harbor, Maine, United States of America., Flanagan RM; Center for Genomics & Systems Biology, New York University, New York, New York, United States of America., Bonnet FX; The MDI Biological Laboratory, Bar Harbor, Maine, United States of America., Piano F; Center for Genomics & Systems Biology, New York University, New York, New York, United States of America.; Center for Genomics & Systems Biology, New York University Abu Dhabi, Abu Dhabi, United Arab Emirates., Ketting RF; Institute of Molecular Biology, Mainz, Germany., Gunsalus KC; Center for Genomics & Systems Biology, New York University, New York, New York, United States of America.; Center for Genomics & Systems Biology, New York University Abu Dhabi, Abu Dhabi, United Arab Emirates., Updike DL; The MDI Biological Laboratory, Bar Harbor, Maine, United States of America.
Jazyk: angličtina
Zdroj: PLoS genetics [PLoS Genet] 2022 Jun 03; Vol. 18 (6), pp. e1010245. Date of Electronic Publication: 2022 Jun 03 (Print Publication: 2022).
DOI: 10.1371/journal.pgen.1010245
Abstrakt: LOTUS and Tudor domain containing proteins have critical roles in the germline. Proteins that contain these domains, such as Tejas/Tapas in Drosophila, help localize the Vasa helicase to the germ granules and facilitate piRNA-mediated transposon silencing. The homologous proteins in mammals, TDRD5 and TDRD7, are required during spermiogenesis. Until now, proteins containing both LOTUS and Tudor domains in Caenorhabditis elegans have remained elusive. Here we describe LOTR-1 (D1081.7), which derives its name from its LOTUS and Tudor domains. Interestingly, LOTR-1 docks next to P granules to colocalize with the broadly conserved Z-granule helicase, ZNFX-1. The Tudor domain of LOTR-1 is required for its Z-granule retention. Like znfx-1 mutants, lotr-1 mutants lose small RNAs from the 3' ends of WAGO and mutator targets, reminiscent of the loss of piRNAs from the 3' ends of piRNA precursor transcripts in mouse Tdrd5 mutants. Our work shows that LOTR-1 acts with ZNFX-1 to bring small RNA amplifying mechanisms towards the 3' ends of its RNA templates.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
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