BAIT

HAS1

ATP-dependent RNA helicase HAS1, L000004179, YMR290C
ATP-dependent RNA helicase; involved in the biogenesis of 40S and 60S ribosome subunits; localizes to both the nuclear periphery and nucleolus; highly enriched in nuclear pore complex fractions; constituent of 66S pre-ribosomal particles
Saccharomyces cerevisiae (S288c)
PREY

RCM1

YNL022C
rRNA m5C methyltransferase; methylates cytosine at position 2278 of 25S rRNA while Nop2p methylates cytosine at position 2870; contains seven beta-strand methyltransferase motif; localized to the nucleolus; interacts with Trm112p; homolog of NSUN5A, a human gene which is deleted in Williams-Beuren Syndrome
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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

At least two molecules of the RNA helicase Has1 are simultaneously present in pre-ribosomes during ribosome biogenesis.

Gnanasundram SV, Kos-Braun IC, Kos M

The RNA helicase Has1 is involved in the biogenesis of both small and large ribosomal subunits. How it performs these separate roles is not fully understood. Here we provide evidence that at least two molecules of Has1 are temporarily present at the same time in 90S pre-ribosomes. We identified multiple Has1 binding sites in the 18S, 5.8S and 25S rRNAs. ... [more]

Nucleic Acids Res. Dec. 18, 2018; 47(20);10852-10864 [Pubmed: 31511893]

Throughput

  • High Throughput

Curated By

  • BioGRID