Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.

Retrotransposition of the budding yeast long terminal repeat retrotransposon Ty3 is activated during mating. In this study, proteins that associate with Ty3 Gag3 capsid protein during virus-like particle (VLP) assembly were identified by mass spectrometry and screened for roles in mating-stimulated...

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Main Authors: Virginia Bilanchone, Kristina Clemens, Robyn Kaake, Anthony R Dawson, Dina Matheos, Kunio Nagashima, Parth Sitlani, Kurt Patterson, Ivan Chang, Lan Huang, Suzanne Sandmeyer
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS Genetics
Online Access:http://europepmc.org/articles/PMC4589538?pdf=render
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author Virginia Bilanchone
Kristina Clemens
Robyn Kaake
Anthony R Dawson
Dina Matheos
Kunio Nagashima
Parth Sitlani
Kurt Patterson
Ivan Chang
Lan Huang
Suzanne Sandmeyer
author_facet Virginia Bilanchone
Kristina Clemens
Robyn Kaake
Anthony R Dawson
Dina Matheos
Kunio Nagashima
Parth Sitlani
Kurt Patterson
Ivan Chang
Lan Huang
Suzanne Sandmeyer
author_sort Virginia Bilanchone
collection DOAJ
description Retrotransposition of the budding yeast long terminal repeat retrotransposon Ty3 is activated during mating. In this study, proteins that associate with Ty3 Gag3 capsid protein during virus-like particle (VLP) assembly were identified by mass spectrometry and screened for roles in mating-stimulated retrotransposition. Components of RNA processing bodies including DEAD box helicases Dhh1/DDX6 and Ded1/DDX3, Sm-like protein Lsm1, decapping protein Dcp2, and 5' to 3' exonuclease Xrn1 were among the proteins identified. These proteins associated with Ty3 proteins and RNA, and were required for formation of Ty3 VLP retrosome assembly factories and for retrotransposition. Specifically, Dhh1/DDX6 was required for normal levels of Ty3 genomic RNA, and Lsm1 and Xrn1 were required for association of Ty3 protein and RNA into retrosomes. This role for components of RNA processing bodies in promoting VLP assembly and retrotransposition during mating in a yeast that lacks RNA interference, contrasts with roles proposed for orthologous components in animal germ cell ribonucleoprotein granules in turnover and epigenetic suppression of retrotransposon RNAs.
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spelling doaj.art-aa70de8f420a474d95b9d993c5f5be992022-12-22T01:26:46ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042015-01-01119e100552810.1371/journal.pgen.1005528Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.Virginia BilanchoneKristina ClemensRobyn KaakeAnthony R DawsonDina MatheosKunio NagashimaParth SitlaniKurt PattersonIvan ChangLan HuangSuzanne SandmeyerRetrotransposition of the budding yeast long terminal repeat retrotransposon Ty3 is activated during mating. In this study, proteins that associate with Ty3 Gag3 capsid protein during virus-like particle (VLP) assembly were identified by mass spectrometry and screened for roles in mating-stimulated retrotransposition. Components of RNA processing bodies including DEAD box helicases Dhh1/DDX6 and Ded1/DDX3, Sm-like protein Lsm1, decapping protein Dcp2, and 5' to 3' exonuclease Xrn1 were among the proteins identified. These proteins associated with Ty3 proteins and RNA, and were required for formation of Ty3 VLP retrosome assembly factories and for retrotransposition. Specifically, Dhh1/DDX6 was required for normal levels of Ty3 genomic RNA, and Lsm1 and Xrn1 were required for association of Ty3 protein and RNA into retrosomes. This role for components of RNA processing bodies in promoting VLP assembly and retrotransposition during mating in a yeast that lacks RNA interference, contrasts with roles proposed for orthologous components in animal germ cell ribonucleoprotein granules in turnover and epigenetic suppression of retrotransposon RNAs.http://europepmc.org/articles/PMC4589538?pdf=render
spellingShingle Virginia Bilanchone
Kristina Clemens
Robyn Kaake
Anthony R Dawson
Dina Matheos
Kunio Nagashima
Parth Sitlani
Kurt Patterson
Ivan Chang
Lan Huang
Suzanne Sandmeyer
Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.
PLoS Genetics
title Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.
title_full Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.
title_fullStr Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.
title_full_unstemmed Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.
title_short Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.
title_sort ty3 retrotransposon hijacks mating yeast rna processing bodies to infect new genomes
url http://europepmc.org/articles/PMC4589538?pdf=render
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