University of Massachusetts Medical School Faculty Publications


RNA recognition by the Caenorhabditis elegans oocyte maturation determinant OMA-1

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date


Document Type



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

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

The Journal of biological chemistry

PubMed ID