title: Widespread changes in the posttranscriptional landscape at the Drosophila oocyte-to-embryo transition.
abstract: The oocyte-to-embryo transition marks the onset of development. The initial phase of this profound change from the differentiated oocyte to the totipotent embryo occurs in the absence of both transcription and mRNA degradation. Here we combine global polysome profiling, ribosome-footprint profiling, and quantitative mass spectrometry in a comprehensive approach to delineate the translational and proteomic changes that occur during this important transition in Drosophila. Our results show that PNG kinase is a critical regulator of the extensive changes in the translatome, acting uniquely at this developmental window. Analysis of the proteome in png mutants provided insights into the contributions of translation to changes in protein levels, revealing a compensatory dynamic between translation and protein turnover during proteome remodeling at the return to totipotency. The proteome changes additionally suggested regulators of meiosis and early embryogenesis, including the conserved H3K4 demethylase LID, which we demonstrated is required during this period despite transcriptional inactivity.
authors.affiliation: Whitehead Institute, Cambridge, MA 02142, USA.
authors.forename: Iva
authors.initials: I
authors.lastname: Kronja
authors.affiliation: Whitehead Institute, Cambridge, MA 02142, USA.
authors.forename: Bingbing
authors.initials: B
authors.lastname: Yuan
authors.affiliation: Whitehead Institute, Cambridge, MA 02142, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
authors.forename: Stephen W
authors.initials: SW
authors.lastname: Eichhorn
authors.affiliation: European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
authors.forename: Kristina
authors.initials: K
authors.lastname: Dzeyk
authors.affiliation: European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
authors.forename: Jeroen
authors.initials: J
authors.lastname: Krijgsveld
authors.affiliation: Whitehead Institute, Cambridge, MA 02142, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
authors.forename: David P
authors.initials: DP
authors.lastname: Bartel
authors.affiliation: Whitehead Institute, Cambridge, MA 02142, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. Electronic address: weaver@wi.mit.edu.
authors.forename: Terry L
authors.initials: TL
authors.lastname: Orr-Weaver
mesh_terms: D000818:Animals; D004330:Drosophila / Q000196:embryology / Q000235:genetics / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental; D056466:Histone Demethylases / Q000235:genetics / Q000378:metabolism; D009865:Oocytes / Q000378:metabolism; D011132:Polyribosomes / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D055550:Protein Stability; D020543:Proteome / Q000235:genetics / Q000378:metabolism*; D012323:RNA Processing, Post-Transcriptional; D020871:RNA Stability; D012333:RNA, Messenger / Q000378:metabolism
chemical_list: D029721:Drosophila Proteins; D020543:Proteome; D012333:RNA, Messenger; D056466:Histone Demethylases; C518655:Lid protein, Drosophila; C417221:png protein, Drosophila; D017346:Protein Serine-Threonine Kinases