Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding

Autor: Ornella Bimai, Ipsita Banerjee, Inna Rozman Grinberg, Ping Huang, Lucas Hultgren, Simon Ekström, Daniel Lundin, Britt-Marie Sjöberg, Derek T Logan

Publikováno v: eLife, Vol 12 (2024)

A small, nucleotide-binding domain, the ATP-cone, is found at the N-terminus of most ribonucleotide reductase (RNR) catalytic subunits. By binding adenosine triphosphate (ATP) or deoxyadenosine triphosphate (dATP) it regulates the enzyme activity of

Externí odkaz: https://doaj.org/article/58c8ed64ca754d1ea6c8072d269703e7

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

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

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)

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

Externí odkaz: https://doaj.org/article/c11cf65babe14228a3e8ad1e379ec405

A subclass of archaeal U8-tRNA sulfurases requires a [4Fe-4S] cluster for catalysis

Autor: Nisha He, Jingjing Zhou, Ornella Bimai, Jonathan Oltmanns, Jean-Luc Ravanat, Christophe Velours, Volker Schünemann, Marc Fontecave, Béatrice Golinelli-Pimpaneau

Publikováno v: Nucleic Acids Research
Nucleic Acids Research, 2022, 50 (22), pp.12969-12978. ⟨10.1093/nar/gkac1156⟩

Sulfuration of uridine 8, in bacterial and archaeal tRNAs, is catalyzed by enzymes formerly known as ThiI, but renamed here TtuI. Two different classes of TtuI proteins, which possess a PP-loop-containing pyrophosphatase domain that includes a conser

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5df5df32ee9d46457ac8eac749549d2
https://pubmed.ncbi.nlm.nih.gov/36533440

Structure-based mechanistic insights into catalysis by tRNA thiolation enzymes

Autor: Simon Arragain, Ornella Bimai, Béatrice Golinelli-Pimpaneau

Publikováno v: Current Opinion in Structural Biology
Current Opinion in Structural Biology, Elsevier, 2020, 65, pp.69-78. ⟨10.1016/j.sbi.2020.06.002⟩

International audience; In all domains of life, ribonucleic acid (RNA) maturation includes post-transcriptional chemical modifications of nucleosides. Many sulfur-containing nucleosides have been identified in transfer RNAs (tRNAs), such as the deriv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab3d0ec7d1298cbd452240549c1aa0a3
https://hal.archives-ouvertes.fr/hal-02945297/file/Revue-thiolation-enzymes-COSB+supp-2020.pdf

Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster

Autor: Sylvain Caillat, Béatrice Golinelli-Pimpaneau, Nadia Touati, Marc Fontecave, Jean-Luc Ravanat, Simon Arragain, Laurent Binet, Ornella Bimai, Mohamed G. Atta, Pierre Legrand

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2017, 114 (28), pp.7355-7360. ⟨10.1073/pnas.1700902114⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2017, 114 (28), pp.7355-7360. ⟨10.1073/pnas.1700902114⟩

International audience; Sulfur is present in several nucleosides within tRNAs. In particular, thiolation of the universally conserved methyl-uridine at position 54 stabilizes tRNAs from thermophilic bacteria and hyperthermo-philic archaea and is requ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6d7812e6a3db97cf856e2cefd9f4ce0
https://hal.science/hal-02410958/document