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Nucleic Acids Research, 1994, Vol. 22, No. 22 4796-4797
© 1994

RNA

Depfining a novel ribonucleotide reductase r1 mRNA cis element that binds to an unique cytoplasmic trans-acting protein

Frank Y. Chen, Francis M. Amara and Jim A. Wright*

Manitoba Institute of Cell Biology, Department of Biochemistry and Molecular Biology, University of Manitoba 100 Olivia Street, Winnipeg, Manitoba R3E 0v9, Canada

*To whom correpsondence should be addressed

Received June 6, 1994. Revised September 6, 1994. Accepted September 6, 1994.

Ribonucleotide reductase is a highly regulated ratelimiting enzyme activity in DNA synthesis, responsible for reducing ribonucleotides to their deoxyribonucleotide forms. Using 3'-end labeled RNA and band-shift and UV cross-linking analyses, we have identified a cis-element, 5'-CAAACUUC-3', within the 3'-utranslated region of the mammalian ribonucleotide reductase R1 mRNA, which binds a cytoplasmic protein in BALB/c 3T3 mouse cells, to form a 57 kDa RNA-protein complex. Sequence-specific binding was observed, and binding was prevented by several different mutations within the cis-element. We suggest that this cis-trans interaction plays a role in R1 mRNA stability.


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