PIWIL3 Forms a Complex with TDRKH in Mammalian Oocytes.

6533b837fe1ef96bd12a29b0

RESEARCH PRODUCT

PIWIL3 Forms a Complex with TDRKH in Mammalian Oocytes.

Minjie Tan Helena T A Van Tol David Rosenkranz Elke F Roovers Mirjam J Damen Tom A E Stout Wei Wu Bernard A J Roelen Afd Biomol.mass Spect. And Proteomics Voortplanting Paard Des/dfah Fr Fah Klinische Reproductie Biomolecular Mass Spectrometry And Proteomics Biomolecular Mass Spectrometry And Proteomics Cs_fertility Cs_cancer

subject

0301 basic medicine Transposable element endocrine system Cytoplasm Arginine transposon Mutagenesis (molecular biology technique)Piwi-interacting RNA Embryonic Development mammal piRNA Biology Mitochondrion Arginine Article 03 medical and health sciences 0302 clinical medicine medicine Animals Amino Acid Sequence RNA Small Interfering oocyte lcsh:QH301-705.5 Gene Gene knockout Muridae genomic integrity PIWI RNA-Binding Proteins General Medicine biology.organism_classification Oocyte Cell biology Mitochondria Protein Transport 030104 developmental biology medicine.anatomical_structure lcsh:Biology (General)Argonaute Proteins Exoribonucleases DNA Transposable Elements Oocytes Cattle 030217 neurology & neurosurgery Function (biology)Protein Binding

description

P-element induced wimpy testis (PIWIs) are crucial guardians of genome integrity, particularly in germ cells. While mammalian PIWIs have been primarily studied in mouse and rat, a homologue for the human PIWIL3 gene is absent in the Muridae family, and hence the unique function of PIWIL3 in germ cells cannot be effectively modeled by mouse knockouts. Herein, we investigated the expression, distribution, and interaction of PIWIL3 in bovine oocytes. We localized PIWIL3 to mitochondria, and demonstrated that PIWIL3 expression is stringently controlled both spatially and temporally before and after fertilization. Moreover, we identified PIWIL3 in a mitochondrial-recruited three-membered complex with Tudor and KH domain-containing protein (TDRKH) and poly(A)-specific ribonuclease-like domain containing 1 (PNLDC1), and demonstrated by mutagenesis that PIWIL3 N-terminal arginines are required for complex assembly. Finally, we sequenced the piRNAs bound to PIWIL3-TDRKH-PNLDC1 and report here that about 50% of these piRNAs map to transposable elements, recapitulating the important role of PIWIL3 in maintaining genome integrity in mammalian oocytes.

year	journal	country	edition	language
2019-07-31	Cells

10.3390/cells9061356 https://pubmed.ncbi.nlm.nih.gov/32486081