BAIT

CSM1

S000007653, YCR086W
Nucleolar protein that mediates homolog segregation during meiosis I; forms a complex with Lrs4p and then Mam1p at kinetochores; required for condensin recruitment to the replication fork barrier site and rDNA repeat segregation
GO Process (4)
GO Function (0)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

MCM10

DNA43, L000000512, YIL150C
Essential chromatin-associated protein; involved in the initiation of DNA replication; required for the association of the MCM2-7 complex with replication origins; required to stabilize the catalytic subunit of DNA polymerase-alpha
Saccharomyces cerevisiae (S288c)

Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

A protein interaction map of the mitotic spindle.

Wong J, Nakajima Y, Westermann S, Shang C, Kang JS, Goodner C, Houshmand P, Fields S, Chan CS, Drubin D, Barnes G, Hazbun T

The mitotic spindle consists of a complex network of proteins that segregates chromosomes in eukaryotes. To strengthen our understanding of the molecular composition, organization, and regulation of the mitotic spindle, we performed a system-wide two-hybrid screen on 94 proteins implicated in spindle function in Saccharomyces cerevisiae. We report 604 predominantly novel interactions that were detected in multiple screens, involving 303 ... [more]

Mol. Biol. Cell Oct. 01, 2007; 18(10);3800-9 [Pubmed: 17634282]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CSM1 MCM10
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.2197BioGRID
2031646

Curated By

  • BioGRID