Chen F Y, Amara F M, Wright J A
Manitoba Institute of Cell Biology, Department of Biochemistry and Molecular Biology, University of Manitoba, Winnipeg, Canada.
Nucleic Acids Res. 1994 Nov 11;22(22):4796-7. doi: 10.1093/nar/22.22.4796.
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.
核糖核苷酸还原酶是DNA合成中一种受到高度调控的限速酶活性,负责将核糖核苷酸还原为脱氧核糖核苷酸形式。利用3'端标记的RNA以及凝胶迁移和紫外线交联分析,我们在哺乳动物核糖核苷酸还原酶R1 mRNA的3'非翻译区内鉴定出一个顺式元件5'-CAAACUUC-3',它在BALB/c 3T3小鼠细胞中与一种细胞质蛋白结合,形成一个57 kDa的RNA-蛋白质复合物。观察到了序列特异性结合,并且顺式元件内的几种不同突变可阻止这种结合。我们认为这种顺式-反式相互作用在R1 mRNA稳定性中发挥作用。