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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Nucleic Acids Research

Trypanosoma brucei RRP44: a versatile enzyme for processing structured and non-structured RNA substrates

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nucleic Acids Research - 11 Jan 2023

Giovanna Cesaro, Heloisa Tramontin da Soler, Eloise Pavāo Guerra-Slompo, Ahmed Haouz, Pierre Legrand, Nilson Ivo Tonin Zanchin and Beatriz Gomes Guimaraes

Link to Pubmed [PMID] – 36583334

Link to DOI – 10.1093/nar/gkac1199

Nucleic Acids Res . 2023 Jan 11;51(1):380-395. doi: 10.1093/nar/gkac1199.

Rrp44/Dis3 is a conserved eukaryotic ribonuclease that acts on processing and degradation of nearly all types of RNA. It contains an endo- (PIN) and an exonucleolytic (RNB) domain and, its depletion in model organisms supports its essential function
for cell viability. In Trypanosoma brucei, depletion of Rrp44 (TbRRP44) blocks maturation of ribosomal RNA, leading to disruption of ribosome synthesis and inhibition of cell proliferation. We have determined the crystal structure of the exoribonucleolytic module of TbRRP44 in an active conformation, revealing novel details of the catalytic mechanism of
the RNB domain. For the first time, the position of the second magnesium involved in the two-metalion mechanism was determined for a member of the RNase II family. In vitro, TbRRP44 acts preferentially on non-structured uridine-rich RNA substrates. However, we demonstrated for the first time that both TbRRP44 and its homologue from Saccharomyces cerevisiae can also degrade structured substrates without 3’-end overhang, suggesting that Rrp44/Dis3 ribonucleases may be involved in degradation of a
wider panel of RNA than has been assumed. Interestingly, deletion of TbRRP44 PIN domain impairs RNA binding to different extents, depending on the type of substrate.