Open AccessDepfining a novel ribonucleotide reductase r1 mRNAciselement that binds to an unique cytoplasmictrans-acting protein
Author(s) -
Youhua Chen,
Francis M. Amara,
Jim A. Wright
Publication year - 1994
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/22.22.4796
Subject(s) - biology , ribonucleotide reductase , ribonucleotide , cytoplasm , messenger rna , microbiology and biotechnology , biochemistry , gene , nucleotide , protein subunit
Ribonucleotide reductase is a highly regulated rate-limiting 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'-untranslated 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.