Depfining a novel ribonucleotide reductase r1 mRNAciselement that binds to an unique cytoplasmictrans-acting protein | Zendy

Frank Chen | Zendy; Francis Amara | Zendy; James R. Wright | Zendy

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Depfining a novel ribonucleotide reductase r1 mRNAciselement that binds to an unique cytoplasmictrans-acting protein

Author(s) -

Frank Chen,

Francis Amara,

James R. 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.

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