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Molecular and Cellular Biology, June 2005, p. 4615-4624, Vol. 25, No. 11
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.11.4615-4624.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mice Deficient in Oocyte-Specific Oligoadenylate Synthetase-Like Protein OAS1D Display Reduced Fertility{dagger}

Wei Yan,1,2 Lang Ma,1 Paula Stein,3 Stephanie A. Pangas,1,4 Kathleen H. Burns,1,{ddagger} Yuchen Bai,5 Richard M. Schultz,3 and Martin M. Matzuk1,4,6*

Departments of Pathology,1 Molecular and Cellular Biology,4 Molecular and Human Genetics, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030,6 Department of Physiology and Cell Biology, University of Nevada School of Medicine, Reno, Nevada 89557,2 Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104,3 Wyeth Research, Collegeville, Pennsylvania 194265

Received 15 November 2004/ Returned for modification 16 December 2004/ Accepted 2 March 2005

The double-stranded RNA (dsRNA)-induced interferon response is a defense mechanism against viral infection. Upon interferon activation by dsRNA, 2',5'-oligoadenylate synthetase 1 (OAS1A) is induced; it binds dsRNA and converts ATP into 2',5'-linked oligomers of adenosine (called 2-5A), which activate RNase L that in turn degrades viral and cellular RNAs. In a screen to identify oocyte-specific genes, we identified a novel murine cDNA encoding an ovary-specific 2',5'-oligoadenylate synthetase-like protein, OAS1D, which displays 59% identity with OAS1A. OAS1D is predominantly cytoplasmic and is exclusively expressed in growing oocytes and early embryos. Like OAS1A, OAS1D binds the dsRNA mimetic poly(I-C), but unlike OAS1A, it lacks 2'-5' adenosine linking activity. OAS1D interacts with OAS1A and inhibits the enzymatic activity of OAS1A. Mutant mice lacking OAS1D (Oas1d–/–) display reduced fertility due to defects in ovarian follicle development, decreased efficiency of ovulation, and eggs that are fertilized arrest at the one-cell stage. These effects are exacerbated after activation of the interferon/OAS1A/RNase L pathway by poly(I-C). We propose that OAS1D suppresses the interferon/OAS/RNase L-mediated cellular destruction by interacting with OAS1A during oogenesis and early embryonic development.

* Corresponding author. Mailing address: Department of Pathology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Phone: (713) 798-6451. Fax: (713) 798-5833. E-mail: mmatzuk{at}bcm.tmc.edu.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} Present address: Department of Pathology, Johns Hopkins School of Medicine, Baltimore, MD 21287.

Molecular and Cellular Biology, June 2005, p. 4615-4624, Vol. 25, No. 11
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.11.4615-4624.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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