Proteomics,Multiomics

Dataset Information

0

Bacillus subtilis RNase M5 cleaves dsRNA in two steps via a two Mg2+-ion dependent mechanism


ABSTRACT: Here, we present the crystal structure of the catalytic domain of M5 bound to two magnesium ions, which reveals the role of each catalytic site acidic residue in metal binding. We further use hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS) to investigate the possibility of structural rearrangements that would allow cleavage of the 5’-strand, and use small-angle X-ray scattering (SAXS) to study the M5 binding to the pre-5S rRNA substrate. This study provides new details on the M5 mechanism used for cleavage of the dsRNA substrate, which proceeds via two metal ions and structural rearrangements of both M5 and the pre-5S rRNA substrate.

INSTRUMENT(S): SYNAPT G2-Si

ORGANISM(S): Geobacillus Stearothermophilus

SUBMITTER: Maxime BOURGUET  

LAB HEAD: Sarah CIANFERANI

PROVIDER: PXD019202 | Pride | 2021-02-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Cluster_data_M5_vs_M5-L18-RNA.csv Csv
Dataset_M5-L18-RNA_state.zip Other
Dataset_M5_state.zip Other
Dataset_final_peptide.zip Other
HD_plots.pptx Other
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