BAIT

RRP5

L000003232, YMR229C
RNA binding protein involved in synthesis of both 18S and 5.8S rRNAs; component of both the ribosomal small subunit (SSU) processosome and the 90S preribosome; acts as part of a Mak21p-Noc2p-Rrp5p module that associates with nascent pre-rRNA during transcription and has a role in bigenesis of the large ribosomal subunit; has binding preference for single stranded tracts of U's; relocalizes from nucleolus to nucleus upon DNA replication stress
Saccharomyces cerevisiae (S288c)
PREY

RLP7

RPL7, L000001647, YNL002C
Nucleolar protein similar to large ribosomal subunit L7 proteins; constituent of 66S pre-ribosomal particles; plays an essential role in processing of precursors to the large ribosomal subunit RNAs; binds junction of ITS2 and ITS2-proximal stem between the 3' end of 5.8S rRNA and the 5' end of 25S rRNA
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

Rrp5p, Noc1p and Noc2p form a protein module which is part of early large ribosomal subunit precursors in S. cerevisiae.

Hierlmeier T, Merl J, Sauert M, Perez-Fernandez J, Schultz P, Bruckmann A, Hamperl S, Ohmayer U, Rachel R, Jacob A, Hergert K, Deutzmann R, Griesenbeck J, Hurt E, Milkereit P, Bassler J, Tschochner H

Eukaryotic ribosome biogenesis requires more than 150 auxiliary proteins, which transiently interact with pre-ribosomal particles. Previous studies suggest that several of these biogenesis factors function together as modules. Using a heterologous expression system, we show that the large ribosomal subunit (LSU) biogenesis factor Noc1p of Saccharomyces cerevisiae can simultaneously interact with the LSU biogenesis factor Noc2p and Rrp5p, a factor ... [more]

Nucleic Acids Res. Jan. 01, 2013; 41(2);1191-1210 [Pubmed: 23209026]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RLP7 RRP5
Affinity Capture-MS
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.

High-BioGRID
-
RRP5 RLP7
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

High-BioGRID
-

Curated By

  • BioGRID