Year: 2013
Type: article
Abstract: 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. Background: OMA-1 is required for oocyte maturation and may function by regulating maternal mRNAs. Results: OMA-1 binds with high affinity to UA(A/U) motifs and regulates glp-1 via its 3′-UTR in live worms. Conclusion: OMA-1 is a sequence-specific RNA-binding protein that represses maternal mRNAs during oocyte maturation. Significance: This work reveals the nature of OMA-1 RNA binding activity, which will help identify targets that contribute to the maturation defective phenotype.
Source: Journal of Biological Chemistry
Authors: Ebru Kaymak, Sean P. Ryder
Institution: University of Massachusetts Chan Medical School
Language: English
Topic: RNA Research and Splicing
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2085668780