Depfining a novel ribonucleotide reductase r1 mRNA cis element that binds to an unique cytoplasmic trans -acting protein
FY Chen, FM Amara, JA Wright - Nucleic acids research, 1994 - academic.oup.com
FY Chen, FM Amara, JA Wright
Nucleic acids research, 1994•academic.oup.comRibonucleotide 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 …
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 …
Abstract
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.
Oxford University Press