Proteomics

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Molecular basis for RanGTP independent disassembly of an importin:ribosomal protein complex by the escortin Tsr2

ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study the complex between the ribosomal protein, eS26A, and the escortin, Tsr2. Cross-linking was performed using different cross-linking chemistries: (1) disuccinimidyl suberate (DSS); (2) a combination of adipic acid dihydrazide (ADH) and the coupling reagent, DMTMM; (3) a combination of pimelic acid dihydrazide (PDH) and the coupling reagent, DMTMM.

INSTRUMENT(S): LTQ Orbitrap, LTQ Orbitrap Elite

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

SUBMITTER: Alexander Leitner  

LAB HEAD: Alexander Leitner

PROVIDER: PXD009106 | Pride | 2018-09-10

REPOSITORIES: Pride

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Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2.

Schütz Sabina S   Michel Erich E   Damberger Fred F FF   Oplová Michaela M   Peña Cohue C   Leitner Alexander A   Aebersold Ruedi R   Allain Frederic H-T FH   Panse Vikram Govind VG  

Nature communications 20180910 1

Disordered extensions at the termini and short internal insertions distinguish eukaryotic ribosomal proteins (r-proteins) from their anucleated archaeal counterparts. Here, we report an NMR structure of such a eukaryotic-specific segment (ESS) in the r-protein eS26 in complex with the escortin Tsr2. The structure reveals how ESS attracts Tsr2 specifically to importin:eS26 complexes entering the nucleus in order to trigger non-canonical RanGTP-independent disassembly. Tsr2 then sequesters the rel  ...[more]

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