Abstract:
:Dihydrofolate reductase (DHFR) is a critical enzyme in de novo purine and thymidylate biosynthesis. An RNA gel mobility shift assay was used to demonstrate a specific interaction between human recombinant DHFR protein and its corresponding DHFR mRNA. Incubation of DHFR protein with either its substrates, dihydrofolate or NADPH, or with an inhibitor, methotrexate, repressed its ability to interact with DHFR mRNA. An in vitro rabbit reticulocyte lysate translation system was used to show that the addition of exogenous human recombinant DHFR protein to in vitro translation reactions specifically inhibited DHFR mRNA translation. These studies suggest that the direct interaction between DHFR protein and its mRNA may be a mechanism for regulation of DHFR synthesis.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Chu E,Takimoto CH,Voeller D,Grem JL,Allegra CJdoi
10.1021/bi00069a009subject
Has Abstractpub_date
1993-05-11 00:00:00pages
4756-60issue
18eissn
0006-2960issn
1520-4995journal_volume
32pub_type
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