RNA recognition by the Caenorhabditis elegans oocyte maturation determinant OMA-1
Department of Biochemistry and Molecular Pharmacology
3' Untranslated Regions; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Carrier Proteins; Female; Oocytes; Oogenesis; RNA, Helminth; Zinc Fingers
Biochemistry | Developmental Biology | Genetics and Genomics
Maternally 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.
DOI of Published Version
J Biol Chem. 2013 Oct 18;288(42):30463-72. doi: 10.1074/jbc.M113.496547. Epub 2013 Sep 6. Link to article on publisher's site
The Journal of biological chemistry
Kaymak, Ebru and Ryder, Sean P., "RNA recognition by the Caenorhabditis elegans oocyte maturation determinant OMA-1" (2013). University of Massachusetts Medical School Faculty Publications. 768.