BAIT

SSB2

YG103, Hsp70 family ATPase SSB2, L000002715, YNL209W
Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; SSB2 has a paralog, SSB1, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

RPL21B

ribosomal 60S subunit protein L21B, L21e, L21B, L000004459, YPL079W
Ribosomal 60S subunit protein L21B; homologous to mammalian ribosomal protein L21, no bacterial homolog; RPL21B has a paralog, RPL21A, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Publication

The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.

Willmund F, del Alamo M, Pechmann S, Chen T, Albanese V, Dammer EB, Peng J, Frydman J

In eukaryotic cells a molecular chaperone network associates with translating ribosomes, assisting the maturation of emerging nascent polypeptides. Hsp70 is perhaps the major eukaryotic ribosome-associated chaperone and the first reported to bind cotranslationally to nascent chains. However, little is known about the underlying principles and function of this interaction. Here, we use a sensitive and global approach to define the ... [more]

Cell Jan. 17, 2013; 152(1);196-209 [Pubmed: 23332755]

Throughput

  • High Throughput

Additional Notes

  • isolation of cotranslationally bound SSB-RNC complexes allows us to identify the chaperone-bound nascent polypeptides through analysis of the mRNAs encoding the substrates

Curated By

  • BioGRID