HSP10 encodes the essential mitochondrial matrix GroES/Cpn10 co-chaperonin that binds Hsp60, regulates the Hsp60 ATPase-driven folding chamber, promotes folding and assembly of imported matrix proteins, and supports sorting of selected proteins such as the Rieske Fe/S protein.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding reviewed for HSP10: ACCEPT. Reason: Retain as the principal biological process supported by Hsp10/Hsp60-dependent folding of imported mitochondrial proteins. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 acts with the mitochondrial chaperonin **Hsp60** to enable ATP-dependent folding and assembly of a subset of imported mitochondrial matrix proteins |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: mitochondrion reviewed for HSP10: ACCEPT. Reason: Retain as broad mitochondrial localization. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md The yeast Hsp10 studied by Hohfeld & Hartl is a **mitochondrial** factor purified from mitochondria and investigated using isolated mitochondria import/folding/sorting assays |
| GO:0005759 mitochondrial matrix | IBA GO_REF:0000033 | ACCEPT | Summary: mitochondrial matrix reviewed for HSP10: ACCEPT. Reason: Retain as the precise core location for Hsp10 action with mitochondrial Hsp60. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Dubaquie et al. explicitly frame yeast hsp10 as a mitochondrial (matrix) co-chaperonin acting with hsp60 in folding of imported proteins |
| GO:0051087 protein-folding chaperone binding | IBA GO_REF:0000033 | ACCEPT | Summary: protein-folding chaperone binding reviewed for HSP10: ACCEPT. Reason: Retain because Hsp10 physically and functionally binds the protein-folding chaperone Hsp60. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md yeast hsp10 is a heptameric co-chaperonin that binds nucleotide-dependently to the 14-mer hsp60 chaperonin |
| GO:0046872 metal ion binding | IBA GO_REF:0000033 | REMOVE | Summary: metal ion binding reviewed for HSP10: REMOVE. Reason: Remove; no reviewed yeast Hsp10 evidence supports independent metal-ion binding as part of its GroES-like co-chaperonin function. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 is the **co-chaperonin** partner of Group I chaperonins |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: unfolded protein binding reviewed for HSP10: MODIFY. Reason: Hsp10 primarily binds the Hsp60 chaperonin lid interface rather than generic unfolded substrates; protein-folding chaperone binding is more accurate. Proposed replacements: protein-folding chaperone binding Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md yeast hsp10 is a heptameric co-chaperonin that binds nucleotide-dependently to the 14-mer hsp60 chaperonin |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | REMOVE | Summary: ATP binding reviewed for HSP10: REMOVE. Reason: Remove; ATP binding/hydrolysis belongs to Hsp60 in this system, while Hsp10 regulates the Hsp60 ATPase-driven cycle. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 regulates the Hsp60 ATPase-driven folding cycle to promote folding/assembly of a subset of imported matrix proteins |
| GO:0005739 mitochondrion | IEA GO_REF:0000117 | ACCEPT | Summary: mitochondrion reviewed for HSP10: ACCEPT. Reason: Retain as broad mitochondrial localization. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md The yeast Hsp10 studied by Hohfeld & Hartl is a **mitochondrial** factor purified from mitochondria and investigated using isolated mitochondria import/folding/sorting assays |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: mitochondrial matrix reviewed for HSP10: ACCEPT. Reason: Retain as the precise core location for Hsp10 action with mitochondrial Hsp60. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Dubaquie et al. explicitly frame yeast hsp10 as a mitochondrial (matrix) co-chaperonin acting with hsp60 in folding of imported proteins |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: protein folding reviewed for HSP10: ACCEPT. Reason: Retain as the principal biological process supported by Hsp10/Hsp60-dependent folding of imported mitochondrial proteins. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 acts with the mitochondrial chaperonin **Hsp60** to enable ATP-dependent folding and assembly of a subset of imported mitochondrial matrix proteins |
| GO:0044183 protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: protein folding chaperone reviewed for HSP10: ACCEPT. Reason: Retain as the co-chaperonin contribution to mitochondrial protein folding. The final annotation should be interpreted with contributes_to semantics because Hsp10 gates and regulates the Hsp60 folding chamber rather than folding substrates independently. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 forms a lid to create a protected folding chamber and coordinate ATP-driven conformational transitions |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | ACCEPT | Summary: mitochondrion reviewed for HSP10: ACCEPT. Reason: Retain as broad mitochondrial localization. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md The yeast Hsp10 studied by Hohfeld & Hartl is a **mitochondrial** factor purified from mitochondria and investigated using isolated mitochondria import/folding/sorting assays |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: mitochondrion reviewed for HSP10: ACCEPT. Reason: Retain as broad mitochondrial localization. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md The yeast Hsp10 studied by Hohfeld & Hartl is a **mitochondrial** factor purified from mitochondria and investigated using isolated mitochondria import/folding/sorting assays |
| GO:0045041 protein import into mitochondrial intermembrane space | IMP PMID:7913473 Role of the chaperonin cofactor Hsp10 in protein folding and... | KEEP AS NON CORE | Summary: protein import into mitochondrial intermembrane space reviewed for HSP10: KEEP_AS_NON_CORE. Reason: Keep as a supported substrate-specific Rieske Fe/S sorting phenotype, but note the mechanistic nuance that Hsp10 acts in the matrix folding/sorting step for a precursor en route to the intermembrane space rather than as a general IMS import receptor. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 contributes to **sorting** of certain proteins that transit the matrix en route to the intermembrane space, specifically the **Rieske Fe/S protein** |
| GO:0051131 chaperone-mediated protein complex assembly | IMP PMID:7913473 Role of the chaperonin cofactor Hsp10 in protein folding and... | ACCEPT | Summary: chaperone-mediated protein complex assembly reviewed for HSP10: ACCEPT. Reason: Retain as Hsp10 supports productive assembly/folding of imported mitochondrial proteins through the Hsp60 chamber. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 regulates the Hsp60 ATPase-driven folding cycle to promote folding/assembly of a subset of imported matrix proteins |
| GO:0005759 mitochondrial matrix | IDA PMID:7903252 Cloning and disruption of the gene encoding yeast mitochondr... | ACCEPT | Summary: mitochondrial matrix reviewed for HSP10: ACCEPT. Reason: Retain as the precise core location for Hsp10 action with mitochondrial Hsp60. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Dubaquie et al. explicitly frame yeast hsp10 as a mitochondrial (matrix) co-chaperonin acting with hsp60 in folding of imported proteins |
| GO:0006457 protein folding | IDA PMID:7902576 Identification and functional analysis of chaperonin 10, the... | ACCEPT | Summary: protein folding reviewed for HSP10: ACCEPT. Reason: Retain as the principal biological process supported by Hsp10/Hsp60-dependent folding of imported mitochondrial proteins. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 acts with the mitochondrial chaperonin **Hsp60** to enable ATP-dependent folding and assembly of a subset of imported mitochondrial matrix proteins |
| GO:0042026 protein refolding | IDA PMID:9256426 Significance of chaperonin 10-mediated inhibition of ATP hyd... | ACCEPT | Summary: protein refolding reviewed for HSP10: ACCEPT. Reason: Retain based on purified Hsp60/Hsp10 refolding assays and mitochondrial substrate-folding experiments. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md In refolding of denatured mitochondrial malate dehydrogenase, hsp60 plus WT hsp10 yields about **40%** refolding |
| GO:0042026 protein refolding | IMP PMID:9256426 Significance of chaperonin 10-mediated inhibition of ATP hyd... | ACCEPT | Summary: protein refolding reviewed for HSP10: ACCEPT. Reason: Retain based on purified Hsp60/Hsp10 refolding assays and mitochondrial substrate-folding experiments. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md In refolding of denatured mitochondrial malate dehydrogenase, hsp60 plus WT hsp10 yields about **40%** refolding |
| GO:0051082 unfolded protein binding | IDA PMID:7902576 Identification and functional analysis of chaperonin 10, the... | MODIFY | Summary: unfolded protein binding reviewed for HSP10: MODIFY. Reason: Hsp10 primarily binds the Hsp60 chaperonin lid interface rather than generic unfolded substrates; protein-folding chaperone binding is more accurate. Proposed replacements: protein-folding chaperone binding Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Hsp10 primarily binds the Hsp60 chaperonin lid interface rather than generic unfolded substrates |
| GO:0051087 protein-folding chaperone binding | IPI PMID:9256426 Significance of chaperonin 10-mediated inhibition of ATP hyd... | ACCEPT | Summary: protein-folding chaperone binding reviewed for HSP10: ACCEPT. Reason: Retain because Hsp10 physically and functionally binds the protein-folding chaperone Hsp60. Supporting Evidence: file:yeast/HSP10/HSP10-deep-research-falcon.md Binding affinity in the ADP state includes one hsp10 binding event with apparent **Kd ~0.88-0.9 nM** |
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Download this section (compressed HTML)Q: Which imported mitochondrial proteins are most dependent on Hsp10 versus Hsp60 alone under physiological conditions?
Q: What features make the Rieske Fe/S protein and other substrates require Hsp10 during matrix transit and onward sorting?
Experiment: Use an endogenous HSP10 degron or temperature-sensitive allele with quantitative mitochondrial import/folding proteomics to compare solubility, protease resistance, assembly, and sorting of matrix and intermembrane-space-destined substrates.
Hypothesis: Hsp10 dependence is substrate-selective and highest for imported proteins that require chamber-mediated folding or remain folding-competent during matrix transit.
Type: mitochondrial import and folding proteomics
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