The enzyme ribonucleotide reductase is a bottleneck for cancer cell growth.
The enzyme ribonucleotide reductase is a bottleneck for cancer cell growth. Scientists at Winship Cancer Institute of Emory University have identified a way of targeting ribonucleotide reductase that may avoid the toxicity of previous approaches, informing focused drug discovery efforts.
The results were published on July 19 in Nature Communications.
Ribonucleotide reductase controls the supply of DNA building blocks, which cancer cells need in abundance for fast growth. Cancer researchers have long had an interest in ribonucleotide reductase, which converts RNA components (ribonucleotides) into DNA building blocks. Several more traditional chemotherapy drugs, such as hydroxyurea, fludarabine, cladribine and gemcitabine, inhibit ribonucleotide reductase by a different mechanism.
Researchers led by Xingming Deng, MD, PhD, found that one of ribonucleotide reductase’s two parts (RRM2) is regulated by a tag, called acetylation, and identified another enzyme (Kat7) that adds that tag. Acetylation at a particular site inactivates RRM2 by preventing individual molecules of RRM2 from pairing up.
Read more at Emory Health Sciences
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