Proteomics

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Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2


ABSTRACT: Otu2-driven deubiquitylation of ribosomal protein eS7 impacts translational efficiency. Here, authors provide the molecular basis for recognition of monoubiquitinated eS7 on 40S and give mechanistic insights into Otu2’s role in translation reset. In this context quantitative mass spectrometry analyses of OTU2 and UBP3 pulldowns were performed.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Thomas Fröhlich  

LAB HEAD: Thomas Fröhlich

PROVIDER: PXD041573 | Pride | 2023-05-13

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
Obp3_TEV_5_R1.raw Raw
Obp3_TEV_5_R2.raw Raw
Obp3_TEV_6_R1.raw Raw
Obp3_TEV_6_R2.raw Raw
Obp3_TEV_7_R1.raw Raw
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Publications

Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2.

Ikeuchi Ken K   Ivic Nives N   Buschauer Robert R   Cheng Jingdong J   Fröhlich Thomas T   Matsuo Yoshitaka Y   Berninghausen Otto O   Inada Toshifumi T   Becker Thomas T   Beckmann Roland R  

Nature communications 20230512 1


In actively translating 80S ribosomes the ribosomal protein eS7 of the 40S subunit is monoubiquitinated by the E3 ligase Not4 and deubiquitinated by Otu2 upon ribosomal subunit recycling. Despite its importance for translation efficiency the exact role and structural basis for this translational reset is poorly understood. Here, structural analysis by cryo-electron microscopy of native and reconstituted Otu2-bound ribosomal complexes reveals that Otu2 engages 40S subunits mainly between ribosome  ...[more]

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