Specific binding of human dihydrofolate reductase protein to dihydrofolate reductase messenger RNA in vitro.

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

Biochemistry

journal_title

Biochemistry

authors

Chu E,Takimoto CH,Voeller D,Grem JL,Allegra CJ

doi

10.1021/bi00069a009

subject

Has Abstract

pub_date

1993-05-11 00:00:00

pages

4756-60

issue

18

eissn

0006-2960

issn

1520-4995

journal_volume

32

pub_type

杂志文章