RRC ID 81883
Author Nishida KM, Okada TN, Kawamura T, Mituyama T, Kawamura Y, Inagaki S, Huang H, Chen D, Kodama T, Siomi H, Siomi MC.
Title Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in Drosophila germlines.
Journal EMBO J
Abstract In Drosophila, the PIWI proteins, Aubergine (Aub), AGO3, and Piwi are expressed in germlines and function in silencing transposons by associating with PIWI-interacting RNAs (piRNAs). Recent studies show that PIWI proteins contain symmetric dimethyl-arginines (sDMAs) and that dPRMT5/Capsuleen/DART5 is the modifying enzyme. Here, we show that Tudor (Tud), one of Tud domain-containing proteins, associates with Aub and AGO3, specifically through their sDMA modifications and that these three proteins form heteromeric complexes. piRNA precursor-like molecules are detected in these complexes. The expression levels of Aub and AGO3, along with their degree of sDMA modification, were not changed by tud mutations. However, the population of transposon-derived piRNAs associated with Aub and AGO3 was altered by tud mutations, whereas the total amounts of small RNAs on Aub and AGO3 was increased. Loss of dprmt5 did not change the stability of Aub, but impaired its association with Tud and lowered piRNA association with Aub. Thus, in germline cells, piRNAs are quality-controlled by dPRMT5 that modifies PIWI proteins, in tight association with Tud.
Volume 28(24)
Pages 3820-31
Published 2009-12-16
DOI 10.1038/emboj.2009.365
PII emboj2009365
PMID 19959991
PMC PMC2797066
MeSH Amino Acid Sequence Animals Arginine / analogs & derivatives Arginine / chemistry Chromatography, Liquid / methods Databases, Protein Drosophila Proteins / metabolism* Drosophila melanogaster / metabolism* Gene Expression Regulation Mass Spectrometry / methods Membrane Transport Proteins / metabolism* Molecular Sequence Data Mutation Protein Methyltransferases / metabolism* Protein-Arginine N-Methyltransferases RNA Interference Sequence Homology, Amino Acid
IF 9.889
Resource
Drosophila 10016Ab-1