Tudor-domain containing proteins act to make the piRNA pathways more robust in Drosophila

Kaoru Sato, Yuka W. Iwasaki, Haruhiko Siomi, Mikiko C. Siomi

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

PIWI-interacting RNAs (piRNAs), a subset of small non-coding RNAs enriched in animal gonads, repress transposons by assembling with PIWI proteins to form potent gene-silencing RNP complexes, piRISCs. Accumulating evidence suggests that piRNAs are produced through three interdependent pathways; the de novo primary pathway, the pingpong pathway, and the phased primary pathway. The de novo primary pathway in Drosophila ovaries produces primary piRNAs for two PIWI members, Piwi and Aub. Aub then initiates the pingpong pathway to produce secondary piRNAs for AGO3. AGO3-slicer dependent cleavage subsequently produces secondary piRNAs for Aub. Trailer products of AGO3-slicer activity are consumed by the phased primary pathway to increase the Piwi-bound piRNA population. All these pathways are regulated by a number of piRNA factors in a highly coordinated fashion. Recent studies show that two Tudor-domain containing piRNA factors, Krimper (Krimp) and Qin/Kumo, play crucial roles in making Aub-AGO3 heterotypic ping-pong robust. This maintains the levels of piRNAs loaded onto Piwi and Aub to efficiently repress transposons at transcriptional and post-transcriptional levels, respectively.

Original languageEnglish
Pages (from-to)86-90
Number of pages5
JournalFly
Volume9
Issue number2
DOIs
Publication statusPublished - 2015 Jan 1

Fingerprint

Drosophila
RNA
proteins
transposons
trailers
gene silencing
gonads
animals

Keywords

  • Krimp
  • Ping-pong
  • PiRNA
  • PIWI
  • Qin
  • Transposon
  • Tudor domain

ASJC Scopus subject areas

  • Insect Science

Cite this

Tudor-domain containing proteins act to make the piRNA pathways more robust in Drosophila. / Sato, Kaoru; Iwasaki, Yuka W.; Siomi, Haruhiko; Siomi, Mikiko C.

In: Fly, Vol. 9, No. 2, 01.01.2015, p. 86-90.

Research output: Contribution to journalArticle

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