Kaymak, EbruRyder, Sean P.2022-08-232022-08-232013-10-182015-10-08J Biol Chem. 2013 Oct 18;288(42):30463-72. doi: 10.1074/jbc.M113.496547. Epub 2013 Sep 6. <a href="http://dx.doi.org/10.1074/jbc.M113.496547">Link to article on publisher's site</a>0021-9258 (Linking)10.1074/jbc.M113.49654724014033https://hdl.handle.net/20.500.14038/30492Maternally supplied mRNAs encode proteins that pattern early embryos in many species. In the nematode Caenorhabditis elegans, a suite of RNA-binding proteins regulates expression of maternal mRNAs during oogenesis, the oocyte to embryo transition, and early embryogenesis. To understand how these RNA-binding proteins contribute to development, it is necessary to determine how they select specific mRNA targets for regulation. OMA-1 and OMA-2 are redundant proteins required for oocyte maturation--an essential part of meiosis that prepares oocytes for fertilization. Both proteins have CCCH type tandem zinc finger RNA-binding domains. Here, we define the RNA binding specificity of OMA-1 and demonstrate that OMA-1/2 are required to repress the expression of a glp-1 3'-UTR reporter in developing oocytes. OMA-1 binds with high affinity to a conserved region of the glp-1 3'-UTR previously shown to interact with POS-1 and GLD-1, RNA-binding proteins required for glp-1 reporter repression in the posterior of fertilized embryos. Our results reveal that OMA-1 is a sequence-specific RNA-binding protein required to repress expression of maternal transcripts during oogenesis and suggest that interplay between OMA-1 and other factors for overlapping binding sites helps to coordinate the transition from oocyte to embryo.en-US3' Untranslated RegionsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCarrier ProteinsFemaleOocytesOogenesisRNA, HelminthZinc FingersBiochemistryDevelopmental BiologyGenetics and GenomicsJournal Articlehttps://escholarship.umassmed.edu/faculty_pubs/7687693419faculty_pubs/768