Société Française de Biochimie et Biologie Moléculaire
Articles of the month
PSTEUR INSTITUTE, PARIS CITÉ UNIVERSITY, Structural Microbiology Unity "Interaction network among de novo purine nucleotide biosynthesis enzymes in Escherichia coli."
FEBS J. doi: 10.1111/febs.16746.
Gedeon A, Karimova G, Ayoub N, Dairou J, Giai Gianetto Q, Vichier-Guerre S, Vidalain PO, Ladant D, Munier-Lehmann H.
Institut de Recherches Cliniques de Montréal (IRCM)
"A rationalized definition of general tumor suppressor microRNAs excluded miR-34a"
Nucleic Acid Res. 50, 4703-4712 DOI:10.1093/nar/gkac277
Mockly S., Houbron E. & Seitz H.
CNRS, Université Paris Cité"Sen1 is a key regulator of transcription-driven conflicts."Molecular Cell. DOI:10.1016/ j.molcel.2022.06.021Aiello U, Challal D, Wentzinger G, Lengronne A, Appanah R, Pasero P, Palancade B, Libri D. (2022)
EMBL, Grenoble "Structural basis for sequence-independent substracte selection by eukaryotic wobble base tRNA deaminase ADAT2/3"
Nature Communication2022, 13, 6737 https://doi.org/10.1038/s41467-022-34441-z
Dolce L.G., Zimmer A.A., Tengo L., Weis F., Rubio M.A.T., Alfonzo J.D. & Kowalinski E.
Cv
Luciano Dolce is a 31 year-old structural biologist. He is interested in RNA editing and modification, with a focus on the protein complexes that perform and regulate them. He did his PhD in Brazil, at the LNBio - Laboratório Nacional de Biociências, applying crystallography and biophysical techniques to study protein-protein complexes. After his PhD, he moved to Grenoble to work as a postdoctoral fellow in Eva Kowalinski's group at EMBL, where he uses Cryo-electron microscopy to better understand RNA editing and modifications in the parasite Trypanosoma brucei.
Contact
Luciano DOLCE
71 avenue des Martyrs
38000 Grenoble
twitter @LgDolce
Résumé de l'article
The essential deamination of adenosine A34 to inosine at the wobble base is the individual tRNA modification with the greatest effects on mRNA decoding, empowering a single tRNA to translate three different codons. To date, many aspects of how eukaryotic deaminases specifically select their multiple substrates remain unclear. Here, using cryo-EM, we present the structure of a eukaryotic ADAT2/3 deaminase bound to a full-length tRNA, revealing that the enzyme distorts the anticodon loop, but in contrast to the bacterial enzymes, selects its substrate via sequence-independent contacts of eukaryote-acquired flexible or intrinsically unfolded motifs distal from the conserved catalytic core. A gating mechanism for substrate entry to the active site is identified. Our multi-step tRNA recognition model yields insights into how RNA editing by A34 deamination evolved, shaped the genetic code, and directly impacts the eukaryotic proteome.
