Starting a new chapter on class Ia ribonucleotide reductases

Talya S Levitz; Catherine L Drennan

doi:10.1016/j.sbi.2022.102489

Starting a new chapter on class Ia ribonucleotide reductases

Curr Opin Struct Biol. 2022 Dec:77:102489. doi: 10.1016/j.sbi.2022.102489. Epub 2022 Oct 19.

Authors

Talya S Levitz¹, Catherine L Drennan²

Affiliations

¹ Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. Electronic address: https://twitter.com/@TalyaLevitz.
² Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. Electronic address: cdrennan@mit.edu.

PMID: 36272229
DOI: 10.1016/j.sbi.2022.102489

Abstract

Ribonucleotide reductases (RNRs) use radical-based chemistry to convert ribonucleotides into deoxyribonucleotides, an essential step in DNA biosynthesis and repair. There are multiple RNR classes, the best studied of which is the class Ia RNR that is found in Escherichia coli, eukaryotes including humans, and many pathogenic and nonpathogenic prokaryotes. This review covers recent advances in our understanding of class Ia RNRs, including a recent reporting of a structure of the active state of the E. coli enzyme and the impacts that the structure has had on spurring research into the mechanism of long-range radical transfer. Additionally, the review considers other recent structural and biochemical research on class Ia RNRs and the potential of that work for the development of anticancer and antibiotic therapeutics.

Publication types

Review

MeSH terms

Escherichia coli / genetics
Humans
Ribonucleotide Reductases* / chemistry
Ribonucleotide Reductases* / genetics

Substances

Ribonucleotide Reductases