Proteomics

Dataset Information

0

Puf6 ushers correct rRNA compaction during ribosome assembly


ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study the complex between the nucleolar factor, Puf6, and the yeast 60S ribosome. Disuccinimidyl suberate (DSS) was used as the cross-linking reagent.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Saccharomyces cerevisiae  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Alexander Leitner  

LAB HEAD: Alexander Leitner

PROVIDER: PXD024131 | Pride | 2021-06-28

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Puf6_identifications.xlsx Xlsx
aleitner_C1509_156.raw Raw
aleitner_C1509_157.raw Raw
aleitner_C1509_158.raw Raw
aleitner_C1509_159.raw Raw
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Publications


Productive ribosomal RNA (rRNA) compaction during ribosome assembly necessitates establishing correct tertiary contacts between distant secondary structure elements. Here, we quantify the response of the yeast proteome to low temperature (LT), a condition where aberrant mis-paired RNA folding intermediates accumulate. We show that, at LT, yeast cells globally boost production of their ribosome assembly machinery. We find that the LT-induced assembly factor, Puf6, binds to the nascent catalytic R  ...[more]

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