BAIT

ASH1

DNA-binding transcription repressor ASH1, L000003058, YKL185W
Component of the Rpd3L histone deacetylase complex; zinc-finger inhibitor of HO transcription; mRNA is localized and translated in the distal tip of anaphase cells, resulting in accumulation of Ash1p in daughter cell nuclei and inhibition of HO expression; potential Cdc28p substrate
Saccharomyces cerevisiae (S288c)
PREY

CTI6

RXT1, YPL181W
Component of the Rpd3L histone deacetylase complex; relieves transcriptional repression by binding to the Cyc8p-Tup1p corepressor and recruiting the SAGA complex to the repressed promoter; contains a PHD finger domain
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

Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex.

Carrozza MJ, Florens L, Swanson SK, Shia WJ, Anderson S, Yates J, Washburn MP, Workman JL

Histone deacetylation by Saccharomyces cerevisiae Rpd3 represses genes regulated by the Ash1 and Ume6 DNA-binding proteins. Rpd3 exists in a small 0.6 MDa (Rpd3S) and large 1.2 MDa (Rpd3L) corepressor complex. In this report, we identify by mass spectrometry and MudPIT the subunits of the Rpd3L complex. These included Rpd3, Sds3, Pho23, Dep1, Rxt2, Sin3, Ash1, Ume1, Sap30, Cti6, Rxt3 ... [more]

Biochim. Biophys. Acta Nov. 10, 2005; 1731(2);77-87; discussion 75-6 [Pubmed: 16314178]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ASH1 CTI6
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.

High4BioGRID
3616918
CTI6 ASH1
Co-purification
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.

Low-BioGRID
-

Curated By

  • BioGRID