A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases

Inna Rozman Grinberg; Markel Martínez-Carranza; Ornella Bimai; Ghada Nouaïria; Saher Shahid; Daniel Lundin; Derek T. Logan; Britt-Marie Sjöberg; Pål Stenmark

doi:10.1038/s41467-022-30328-1

Nature Communications (May 2022)

A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases

Inna Rozman Grinberg,
Markel Martínez-Carranza,
Ornella Bimai,
Ghada Nouaïria,
Saher Shahid,
Daniel Lundin,
Derek T. Logan,
Britt-Marie Sjöberg,
Pål Stenmark

Affiliations

Inna Rozman Grinberg: Department of Biochemistry and Biophysics, Stockholm University
Markel Martínez-Carranza: Department of Biochemistry and Biophysics, Stockholm University
Ornella Bimai: Department of Biochemistry and Biophysics, Stockholm University
Ghada Nouaïria: Department of Biochemistry and Biophysics, Stockholm University
Saher Shahid: Department of Biochemistry and Biophysics, Stockholm University
Daniel Lundin: Department of Biochemistry and Biophysics, Stockholm University
Derek T. Logan: Biochemistry and Structural Biology, Department of Chemistry, Lund University
Britt-Marie Sjöberg: Department of Biochemistry and Biophysics, Stockholm University
Pål Stenmark: Department of Biochemistry and Biophysics, Stockholm University

DOI: https://doi.org/10.1038/s41467-022-30328-1
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 10

Abstract

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Ribonucleotide reductase (RNR) is an essential enzyme that catalyzes the synthesis of DNA building blocks. Here, the authors present the cryo-EM structure and mechanism of action of NrdR, the RNR-specific repressor, that controls transcription of RNR genes in bacteria.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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