Structure and Function of the Bacterial Decapping Enzyme NudC

Overview

Journal Nat Chem Biol

Specialties Biochemistry
Biology
Chemistry

Date 2016 Jul 19

PMID 27428510

Citations 35

Authors

Katharina Hofer

Sisi Li

Florian Abele

Jens Frindert

Jasmin Schlotthauer

Julia Grawenhoff

Jiamu Du

Dinshaw J Patel

Andres Jaschke

Affiliations

Soon will be listed here.

Abstract

RNA capping and decapping are thought to be distinctive features of eukaryotes. The redox cofactor NAD was recently discovered to be attached to small regulatory RNAs in bacteria in a cap-like manner, and Nudix hydrolase NudC was found to act as a NAD-decapping enzyme in vitro and in vivo. Here, crystal structures of Escherichia coli NudC in complex with substrate NAD and with cleavage product NMN reveal the catalytic residues lining the binding pocket and principles underlying molecular recognition of substrate and product. Biochemical mutation analysis identifies the conserved Nudix motif as the catalytic center of the enzyme, which needs to be homodimeric, as the catalytic pocket is composed of amino acids from both monomers. NudC is single-strand specific and has a purine preference for the 5'-terminal nucleotide. The enzyme strongly prefers NAD-linked RNA (NAD-RNA) over NAD and binds to a diverse set of cellular RNAs in an unspecific manner.

Citing Articles

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Identification of NAD-RNA species and ADPR-RNA decapping in Archaea.

Gomes-Filho J, Breuer R, Morales-Filloy H, Pozhydaieva N, Borst A, Paczia N Nat Commun. 2023; 14(1):7597.

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