title: Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.
abstract: 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.
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Virginia
authors.initials: V
authors.lastname: Bilanchone
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Kristina
authors.initials: K
authors.lastname: Clemens
authors.affiliation: Department of Physiology and Biophysics, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Robyn
authors.initials: R
authors.lastname: Kaake
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Anthony R
authors.initials: AR
authors.lastname: Dawson
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Dina
authors.initials: D
authors.lastname: Matheos
authors.affiliation: Electron Microscope Laboratory, NCI-Frederick, SAIC-Frederick, Inc., Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States of America.
authors.forename: Kunio
authors.initials: K
authors.lastname: Nagashima
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Parth
authors.initials: P
authors.lastname: Sitlani
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Kurt
authors.initials: K
authors.lastname: Patterson
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Ivan
authors.initials: I
authors.lastname: Chang
authors.affiliation: Department of Physiology and Biophysics, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Lan
authors.initials: L
authors.lastname: Huang
authors.affiliation: Department of Biological Chemistry, University of California, Irvine, Irvine, California, United States of America; Institute for Genomics and Bioinformatics, University of California, Irvine, Irvine, California, United States of America.
authors.forename: Suzanne
authors.initials: S
authors.lastname: Sandmeyer
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism; D053487:DEAD-box RNA Helicases / Q000235:genetics / Q000378:metabolism; D005095:Exoribonucleases / Q000235:genetics / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D016681:Genome, Fungal; D012313:RNA / Q000235:genetics*; D039381:RNA Cap-Binding Proteins / Q000235:genetics / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase / Q000235:genetics; D018626:Retroelements / Q000235:genetics*; D012261:Ribonucleoproteins / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D020079:Terminal Repeat Sequences / Q000235:genetics
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C114069:LSM1 protein, S cerevisiae; C429283:MDV1 protein, S cerevisiae; D039381:RNA Cap-Binding Proteins; D018626:Retroelements; D012261:Ribonucleoproteins; D029701:Saccharomyces cerevisiae Proteins; D012313:RNA; D012194:RNA-Directed DNA Polymerase; D005095:Exoribonucleases; C068398:XRN1 protein, S cerevisiae; C445083:DHH1 protein, S cerevisiae; D053487:DEAD-box RNA Helicases