title: Barentsz is essential for the posterior localization of oskar mRNA and colocalizes with it to the posterior pole.
abstract: The localization of Oskar at the posterior pole of the Drosophila oocyte induces the assembly of the pole plasm and therefore defines where the abdomen and germ cells form in the embryo. This localization is achieved by the targeting of oskar mRNA to the posterior and the localized activation of its translation. oskar mRNA seems likely to be actively transported along microtubules, since its localization requires both an intact microtubule cytoskeleton and the plus end-directed motor kinesin I, but nothing is known about how the RNA is coupled to the motor. Here, we describe barentsz, a novel gene required for the localization of oskar mRNA. In contrast to all other mutations that disrupt this process, barentsz-null mutants completely block the posterior localization of oskar mRNA without affecting bicoid and gurken mRNA localization, the organization of the microtubules, or subsequent steps in pole plasm assembly. Surprisingly, most mutant embryos still form an abdomen, indicating that oskar mRNA localization is partially redundant with the translational control. Barentsz protein colocalizes to the posterior with oskar mRNA, and this localization is oskar mRNA dependent. Thus, Barentsz is essential for the posterior localization of oskar mRNA and behaves as a specific component of the oskar RNA transport complex.
authors.affiliation: Wellcome/CRC Institute, and the Department of Genetics, University of Cambridge, Cambridge CB2 1QR, United Kingdom.
authors.forename: F J
authors.initials: FJ
authors.lastname: van Eeden
authors.forename: I M
authors.initials: IM
authors.lastname: Palacios
authors.forename: M
authors.initials: M
authors.lastname: Petronczki
authors.forename: M J
authors.initials: MJ
authors.lastname: Weston
authors.forename: D
authors.initials: D
authors.lastname: St Johnston
mesh_terms: D000818:Animals; D016764:Cell Polarity / Q000502:physiology; D003001:Cloning, Molecular; D004330:Drosophila; D029721:Drosophila Proteins; D005260:Female; D019476:Insect Proteins / Q000032:analysis / Q000235:genetics* / Q000378:metabolism*; D008297:Male; D008870:Microtubules / Q000502:physiology; D008969:Molecular Sequence Data; D009154:Mutation / Q000502:physiology; D009865:Oocytes / Q000166:cytology / Q000502:physiology; D009866:Oogenesis / Q000502:physiology; D010641:Phenotype; D012150:Polymorphism, Restriction Fragment Length; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D011995:Recombination, Genetic / Q000502:physiology; D017386:Sequence Homology, Amino Acid
chemical_list: D029721:Drosophila Proteins; D019476:Insect Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; C433983:btz protein, Drosophila; C091675:osk protein, Drosophila