BAIT

SMC4

condensin subunit SMC4, L000003472, YLR086W
Subunit of the condensin complex; condensin reorganizes chromosomes during both mitosis and meiosis; forms a subcomplex with Smc2p that has ATP-hydrolyzing and DNA-binding activity, but other condensin subunits are required for chromatin binding; required for tRNA gene clustering at the nucleolus; potential Cdc28p substrate
Saccharomyces cerevisiae (S288c)
PREY

SMC2

condensin subunit SMC2, L000001927, YFR031C
Subunit of the condensin complex; condensin reorganizes chromosomes during both mitosis and meiosis; essential SMC chromosomal ATPase family member that forms a subcomplex with Smc2p that has ATP-hydrolyzing and DNA-binding activity, but other condensin subunits are required for chromatin binding; required for clustering of tRNA genes at the nucleolus
Saccharomyces cerevisiae (S288c)

Synthetic Growth Defect

A genetic interaction is inferred when mutations in separate genes, each of which alone causes a minimal phenotype, result in a significant growth defect under a given condition when combined in the same cell.

Publication

Cooperation of sumoylated chromosomal proteins in rDNA maintenance.

Takahashi Y, Dulev S, Liu X, Hiller NJ, Zhao X, Strunnikov A

SUMO is a posttranslational modifier that can modulate protein activities, interactions, and localizations. As the GFP-Smt3p fusion protein has a preference for subnucleolar localization, especially when deconjugation is impaired, the nucleolar role of SUMO can be the key to its biological functions. Using conditional triple SUMO E3 mutants, we show that defects in sumoylation impair rDNA maintenance, i.e., the rDNA ... [more]

PLoS Genet. Oct. 01, 2008; 4(10);e1000215 [Pubmed: 18846224]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: vegetative growth (APO:0000106)
  • phenotype: heat sensitivity (APO:0000147)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SMC2 SMC4
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
-
SMC4 SMC2
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
-
SMC2 SMC4
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
SMC2 SMC4
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
1518245
SMC2 SMC4
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
-
SMC2 SMC4
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
SMC2 SMC4
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID