BAIT

RPN8

proteasome regulatory particle lid subunit RPN8, L000004308, YOR261C
Essential non-ATPase regulatory subunit of the 26S proteasome; has similarity to the human p40 proteasomal subunit and to another S. cerevisiae regulatory subunit, Rpn11p
GO Process (1)
GO Function (0)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

SEM1

DSS1, HOD1, proteasome regulatory particle lid subunit SEM1, L000003539, L000004647, YDR363W-A
Component of lid subcomplex of 26S proteasome regulatory subunit; involved in mRNA export mediated by TREX-2 complex (Sac3p-Thp1p); assumes different conformations in different contexts, functions as molecular glue stabilizing the Rpn3p/Rpn7p regulatory heterodimer, and tethers it to lid helical bundle; ortholog of human DSS1; protein abundance increases in response to DNA replication stress
Saccharomyces cerevisiae (S288c)

Cross-Linking-MS (XL-MS)

An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).

Publication

High-density chemical cross-linking for modeling protein interactions.

Mintseris J, Gygi SP

Detailed mechanistic understanding of protein complex function is greatly enhanced by insights from its 3-dimensional structure. Traditional methods of protein structure elucidation remain expensive and labor-intensive and require highly purified starting material. Chemical cross-linking coupled with mass spectrometry offers an alternative that has seen increased use, especially in combination with other experimental approaches like cryo-electron microscopy. Here we report advances ... [more]

Proc Natl Acad Sci U S A Jan. 07, 2020; 117(1);93-102 [Pubmed: 31848235]

Throughput

  • Low Throughput

Additional Notes

  • High confidence interactions were identified using the PIXL (Protein Interactions from Cross-Linking) algorithm and stringently filtered to 1% FDR.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SEM1 RPN8
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.

Low-BioGRID
-
SEM1 RPN8
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
-
SEM1 RPN8
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.

High10BioGRID
3612918
SEM1 RPN8
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.

Low-BioGRID
-
RPN8 SEM1
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-0.7034BioGRID
2018725

Curated By

  • BioGRID