Distinct -acting elements mediate targeting and clustering of polar granule mRNAs. Author Whitby Eagle, Daniel Yeboah-Kordieh, Matthew Niepielko, Elizabeth Gavis Publication Year 2018 Type Journal Article Abstract Specification and development of germ cells depend on molecular determinants within the germ plasm, a specialized cytoplasmic domain at the posterior of the embryo. Localization of numerous mRNAs to the germ plasm occurs by their incorporation, as single-transcript ribonucleoprotein (RNP) particles, into complex RNP granules called polar granules. Incorporation of mRNAs into polar granules is followed by recruitment of additional like transcripts to form discrete homotypic clusters. The -acting localization signals that target mRNAs to polar granules and promote homotypic clustering remain largely uncharacterized. Here, we show that the () and () 3' untranslated regions contain complex localization signals comprising multiple, independently weak and partially functionally redundant localization elements (LEs). We demonstrate that targeting of to polar granules and self-assembly into homotypic clusters are functionally separable processes mediated by distinct classes of LEs. We identify a sequence motif shared by other polar granule mRNAs that contributes to homotypic clustering. Our results suggest that mRNA localization signal complexity may be a feature required by the targeting and self-recruitment mechanism that drives germ plasm mRNA localization. Keywords Animals, Drosophila Proteins, Nuclear Proteins, RNA, Messenger, Base Pairing, Conserved Sequence, Drosophila melanogaster, Cell Polarity, Regulatory Sequences, Nucleic Acid, 3' Untranslated Regions, Intercellular Signaling Peptides and Proteins, Cytoplasmic Granules, Positive Transcriptional Elongation Factor B, Nucleotide Motifs Journal Development Volume 145 Issue 22 Date Published 2018 Nov 22 ISSN Number 1477-9129 DOI 10.1242/dev.164657 Alternate Journal Development PMCID PMC6262787 PMID 30333216 PubMedPubMed CentralGoogle ScholarBibTeXEndNote X3 XML