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Originally published In Press as doi:10.1074/jbc.M010833200 on June 22, 2001

J. Biol. Chem., Vol. 276, Issue 33, 30995-31003, August 17, 2001
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Characterization of a General Stabilizer Element That Blocks Deadenylation-dependent mRNA Decay*

Maria J. Ruiz-EchevarriaDagger §, Raj MunshiDagger ||, Julie TombackDagger , Terri Goss Kinzy**Dagger Dagger , and Stuart W. Peltz**§§

From the Dagger  Department of Molecular Genetics and Microbiology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey and the ** Cancer Institute of New Jersey, Piscataway, New Jersey 08854

mRNA degradation is a regulated process that can play an important role in determining the level of expression of specific genes. The rate at which a specific mRNA is degraded depends largely on specific cis-acting sequences located throughout the transcript. cis-Acting destabilizer sequences that promote increased rates of decay have been identified in several short-lived mRNAs. However, little is known about elements that promote stability, known as stabilizer elements (STEs), and how they function. The work presented here describes the characterization of a STE in the PGK1 transcript. The PGK1 stabilizer element (P-STE) has been delineated to a 64-nucleotide sequence from the coding region that can stabilize a chimeric transcript containing the instability elements from the 3'-untranslated region of the MFA2 transcript. The P-STE is located within the PGK1 coding region and functions when located in the translated portion of the transcript and at a minimum distance from the 3'-untranslated region. These results further support the link between translation and mRNA degradation. A conserved sequence in the TEF1/2 transcript has been identified that also functions as a STE, suggesting that this sequence element maybe a general stability determinant found in other yeast mRNAs.


* This work was supported in part by National Institutes of Health Grants GM58276 (to S. W. P) and GM57483 (to T. G. K.), by an American Heart Association Established Investigator award (to S. W. P.), and by an American Heart Association grant-in-aid (to M. J. R.-E.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Current address: Curagen Corp., New Haven, CT 06511.

These authors contributed equally to this work.

|| Supported by a Howard Hughes undergraduate fellowship during part of this research.

Dagger Dagger To whom correspondence may be addressed: Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 675 Hoes Ln., Piscataway, NJ 08854. Tel.: 732-235-5450; Fax: 732-235-5223; E-mail: kinzytg@umdnj.edu.

§§ To whom correspondence may be addressed: Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 675 Hoes Ln., Piscataway, NJ 08854. Tel.: 732-235-4790; Fax: 732-235-5223; E-mail: peltz@umdnj.edu.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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