Complex: PBA3-PBA4 proteasomal chaperone complex
Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.
- Curated by
- UniProt
- ComplexAc
- CPX-8172
- Systematic Name
- IRC25:POC4
- SGD ID
- SGD:S000345854
- Aliases
- Dmp1-Dmp2 complex ; POC3-POC4 chaperone complex
- Description
- Chaperone complex with a role in the early stage assembly of the 26S proteasome (CPX-2262). Binds to the bottom of the alpha ring as it assembles, on the opposite side to the PBA1-PBA2 complex (CPX-8171) and is assumed to enforce the proper configuration of the ring and prevent the premature binding of other complexes which interact with the core barrel-shaped chamber. PBA3-PBA4 appears to disengage shortly after completion of the alpha-ring.
Complex Diagram
This diagram displays the protein subunits (blue) of the complex and how they interact with each other. Interactions with other relevant participants such as small molecules (purple), sub-complexes (yellow), and other subunits (red) are also shown. If a participant appears in the diagram with no lines connected to it, then its specific interactions with other participants are currently unknown.
PDB Structure
When available from the Protein Data Bank (PDB), the physical structure of the macromolecular complex is displayed. Click on the image or link for further information about the physical structure.
| 2Z5B |
Subunits
This table lists all participants of the complex (proteins, small molecules, nucleic acids, etc.) and their respective stoichiometry. A brief description is also provided for each participant in the table.
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| Subunit | Description | Stoichiometry |
|---|
Gene Ontology
Gene Ontology (GO) terms that describe the function of a complex, the biological process in which it participates, or its cellular location. Click on a term for its definition and other objects annotated to that term.
- Molecular Function
-
- enables proteasome binding (IDA)
- Biological Process
-
- involved in proteasome core complex assembly (IDA)
Shared Annotations
This diagram displays Gene Ontology terms (green) and subunits (blue) that are shared between the given macromolecular complex (black) and other yeast complexes (yellow). The shared GO terms or subunits can be visualized separately using the radio button at the bottom of the graph. Note: No diagram is shown ("No shared annotations") if there are less than 2 shared annotations (either GO terms or subunits of other complexes) between this complex and any other complexes.
References
List of references used specifically to curate the information on this page.
- Schnell HM, et al. (2022) Chaperone-mediated assembly of the proteasome core particle - recent developments and structural insights. J Cell Sci 135(8) PMID: 35451017
- Yashiroda H, et al. (2008) Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol 15(3):228-36 PMID: 18278057
- Le Tallec B, et al. (2007) 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol Cell 27(4):660-74 PMID: 17707236
Resources
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