ArticleJournal of bacteriology2008
NrdI essentiality for class Ib ribonucleotide reduction in Streptococcus pyogenes.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
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- Alternating magnetic fields enhance growth and co-production of cellulase and protease in Bacillus velezensis fermentation.Archives of microbiology · 2026Article
- Characterization of a second class Ie ribonucleotide reductase.Communications biology · 2025Article
- Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases in Mycobacteria.Current research in structural biology · 2024Article
- Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.Journal of the American Chemical Society · 2023Article
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
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- Managing Manganese: The Role of Manganese Homeostasis in Streptococcal Pathogenesis.Frontiers in cell and developmental biology · 2022Review
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Class Id ribonucleotide reductase utilizes a MnJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Metal sensing and regulation of adaptive responses to manganese limitation by MtsR is critical for group A streptococcus virulence.Nucleic acids research · 2019Article
- A Research-inspired biochemistry laboratory module-combining expression, purification, crystallization, structure-solving, and characterization of a flavodoxin-like protein.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology · 2019Article
- Article
- Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- An endogenous dAMP ligand inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- PhoU2 but Not PhoU1 as an Important Regulator of Biofilm Formation and Tolerance to Multiple Stresses by Participating in Various Fundamental Metabolic Processes in Staphylococcus epidermidis.Journal of bacteriology · 2017Article
- Role of Ribonucleotide Reductase in Bacillus subtilis Stress-Associated Mutagenesis.Journal of bacteriology · 2017Article
- Ribonucleotide Reductases from Bifidobacteria Contain Multiple Conserved Indels Distinguishing Them from All Other Organisms:Frontiers in microbiology · 2017Article
- Unusual Five Copies and Dual Forms of nrdB in "Candidatus Liberibacter asiaticus": Biological Implications and PCR Detection Application.Scientific reports · 2016Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Streptococcus pyogenes genome harbors two clusters of class Ib ribonucleotide reductase genes, nrdHEF and nrdF*I*E*, and a second stand-alone nrdI gene, designated nrdI2. We show that both clusters are expressed simultaneously as two independent operons. The NrdEF enzyme is functionally active in vitro, while the NrdE*F* enzyme is not. The NrdF* protein lacks three of the six highly conserved iron-liganding side chains and cannot form a dinuclear iron site or a tyrosyl radical. In vivo, on the other hand, both operons are functional in heterologous complementation in Escherichia coli. The nrdF*I*E* operon requires the presence of the nrdI* gene, and the nrdHEF operon gained activity upon cotranscription of the heterologous nrdI gene from Streptococcus pneumoniae, while neither nrdI* nor nrdI2 from S. pyogenes rendered it active. Our results highlight the essential role of the flavodoxin NrdI protein in vivo, and we suggest that it is needed to reduce met-NrdF, thereby enabling the spontaneous reformation of the tyrosyl radical. The NrdI* flavodoxin may play a more direct role in ribonucleotide reduction by the NrdF*I*E* system. We discuss the possibility that the nrdF*I*E* operon has been horizontally transferred to S. pyogenes from Mycoplasma spp.
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