BAIT

NOC4

UTP19, YPR144C
Nucleolar protein; forms a complex with Nop14p that mediates maturation and nuclear export of 40S ribosomal subunits; relocalizes to the cytosol in response to hypoxia
Saccharomyces cerevisiae (S288c)
PREY

FPR4

peptidylprolyl isomerase FPR4, L000004352, YLR449W
Peptidyl-prolyl cis-trans isomerase (PPIase); nuclear proline isomerase; affects expression of multiple genes via its role in nucleosome assembly; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; FPR4 has a paralog, FPR3, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

Structural and functional analysis of ribosome assembly factor Efg1.

Shu S, Ye K

Ribosome biogenesis in eukaryotes is a complicated process that involves association and dissociation of numerous assembly factors and snoRNAs. The yeast small ribosomal subunit is first assembled into 90S pre-ribosomes in an ordered and dynamic manner. Efg1 is a protein with no recognizable domain that is associated with early 90S particles. Here, we determine the crystal structure of Efg1 from ... [more]

Nucleic Acids Res. Jan. 18, 2018; (); [Pubmed: 29361028]

Throughput

  • High Throughput

Curated By

  • BioGRID