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1: Biochem Biophys Res Commun. 2008 May 9;369(3):795-800. Epub 2007 Sep 21.
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Identification of a cis-acting element of human dihydrofolate reductase mRNA.

Tai N, Schmitz JC, Chen TM, O'Neill MB, Chu E.

Department of Medicine and Pharmacology, Developmental Therapeutic Program, Yale Cancer Center, Yale University School of Medicine, New Haven, CT 06520, USA.

Human dihydrofolate reductase (DHFR) is a critical target in cancer chemotherapy. Previous studies showed that an 82-nt RNA fragment within the DHFR mRNA protein-coding region functions as a DHFR cis-acting response element. In this study, we further investigated the key elements contained within this sequence that are required for the DHFR mRNA-DHFR protein interaction. Using enzymatic foot-printing assays and RNA-binding experiments, we isolated a 27-nt sequence (DHFR27, corresponding to nts 407-433), which bound with high affinity and specificity to human DHFR to form a ribonucleoprotein complex. In vivo transient transfection experiments using a luciferase reporter system revealed that DHFR27 RNA could repress the luciferase expression in a DHFR-dependent manner when placed upstream of luciferase mRNA. This work provides new insights into the essential molecular elements that mediate RNA-protein interactions.

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PMID: 18045573 [PubMed - indexed for MEDLINE]