Abstract
Ribonucleotide reductase (RNR) catalyzes the first committed reaction in DNA synthesis. Most of what we know about RNR regulation comes from studies with cultured cells and with purified proteins. In this study, Tran et al. use Cre-Lox technology to inactivate RNR large subunit expression in heart and skeletal muscle of mouse embryos. Analysis of these mutants paints a picture of dNTP regulation in whole animals quite different from that seen in studies of purified proteins and cultured cells.
Highlights
Several years ago, I entitled a preview article comparable with this one “The most interesting enzyme in the world” [1]
Analysis of post-birth survival provided understanding of the ability of salvage pathways and import from other tissues to compensate for the loss of the main de novo route for dNTP synthesis
The Cre-Lox technology used by Tran et al inactivated synthesis of the large (R1) subunit late in embryonic development, leading to progressive loss of active de novo dNTP synthesis— in heart and skeletal muscle
Summary
I entitled a preview article comparable with this one “The most interesting enzyme in the world” [1]. What Tran et al have done is to use Cre-Lox technology to inactivate RNR large subunit expression in heart and skeletal muscle of mouse embryos. Analysis of nucleoside triphosphate pools in these animals (dNTPs and rNTPs) allowed understanding of the regulation of nucleotide synthesis
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