PFD1 encodes the Pfd1/Gim6 beta-type subunit of the cytosolic prefoldin complex, an ATP-independent cochaperone that captures nonnative actin and tubulin folding intermediates and delivers them to CCT/TRiC, with secondary nuclear roles in transcription elongation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md as part of the prefoldin/GimC complex it **captures and stabilizes unfolded actin and tubulin intermediates** and **hands them to CCT/TRiC** |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: unfolded protein binding reviewed for PFD1: MODIFY. Reason: Unfolded protein binding is mechanistically close but too broad; Pfd1 is best represented as a prefoldin protein-folding cochaperone. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin functions largely as an **ATP-independent holdase**, stabilizing folding intermediates and preventing aggregation prior to transfer to CCT/TRiC |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: cytoplasm reviewed for PFD1: ACCEPT. Reason: Retain as the principal cellular compartment for the canonical prefoldin to CCT/TRiC folding pathway. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md The central pathway involving Pfd1 is the **cytosolic folding pipeline** for cytoskeletal proteins |
| GO:0044183 protein folding chaperone | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding chaperone reviewed for PFD1: ACCEPT. Reason: Retain as the best molecular-function term for the ATP-independent prefoldin cochaperone role. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md Pfd1's primary function is **structural/cochaperone activity**, not catalysis |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: cytoplasm reviewed for PFD1: ACCEPT. Reason: Retain as the principal cellular compartment for the canonical prefoldin to CCT/TRiC folding pathway. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md The central pathway involving Pfd1 is the **cytosolic folding pipeline** for cytoskeletal proteins |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md as part of the prefoldin/GimC complex it **captures and stabilizes unfolded actin and tubulin intermediates** and **hands them to CCT/TRiC** |
| GO:0016272 prefoldin complex | IEA GO_REF:0000002 | ACCEPT | Summary: prefoldin complex reviewed for PFD1: ACCEPT. Reason: Retain; Pfd1/Gim6 is a component of the heterohexameric prefoldin complex. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md Canonical eukaryotic prefoldin contains **six distinct subunits (PFD1-PFD6)**, organized as **two alpha-type** and **four beta-type** subunits |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000002 | MODIFY | Summary: unfolded protein binding reviewed for PFD1: MODIFY. Reason: Unfolded protein binding is mechanistically close but too broad; Pfd1 is best represented as a prefoldin protein-folding cochaperone. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin functions largely as an **ATP-independent holdase**, stabilizing folding intermediates and preventing aggregation prior to transfer to CCT/TRiC |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for PFD1: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is too generic for curation; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for PFD1: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is too generic for curation; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for PFD1: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is too generic for curation; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for PFD1: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is too generic for curation; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:9878052 Compartmentation of protein folding in vivo: sequestration o... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for PFD1: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is too generic for curation; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0006457 protein folding | NAS PMID:9463374 A novel protein complex promoting formation of functional al... | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md Yeast prefoldin/GimC physically interacts with TRiC/CCT in vivo and in vitro |
| GO:0032968 positive regulation of transcription elongation by RNA polymerase II | IMP PMID:24068951 The prefoldin complex regulates chromatin dynamics during tr... | KEEP AS NON CORE | Summary: positive regulation of transcription elongation by RNA polymerase II reviewed for PFD1: KEEP_AS_NON_CORE. Reason: Keep as an evidence-supported secondary nuclear/chromatin role, but do not treat it as the core evolved role of Pfd1. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md PFD1 deletion reduces RNAPII occupancy across gene bodies |
| GO:0032968 positive regulation of transcription elongation by RNA polymerase II | IGI PMID:24068951 The prefoldin complex regulates chromatin dynamics during tr... | KEEP AS NON CORE | Summary: positive regulation of transcription elongation by RNA polymerase II reviewed for PFD1: KEEP_AS_NON_CORE. Reason: Keep as an evidence-supported secondary nuclear/chromatin role, but do not treat it as the core evolved role of Pfd1. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md PFD1 deletion reduces RNAPII occupancy across gene bodies |
| GO:0006457 protein folding | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md actin folding by TRiC is slowed ~5-fold compared with wild type |
| GO:0007010 cytoskeleton organization | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | KEEP AS NON CORE | Summary: cytoskeleton organization reviewed for PFD1: KEEP_AS_NON_CORE. Reason: Keep as a downstream consequence of actin/tubulin folding defects rather than the direct molecular role. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md gim deletion mutants exhibit actin and tubulin phenotypes resembling TRiC mutants |
| GO:0016272 prefoldin complex | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | ACCEPT | Summary: prefoldin complex reviewed for PFD1: ACCEPT. Reason: Retain; Pfd1/Gim6 is a component of the heterohexameric prefoldin complex. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md Canonical eukaryotic prefoldin contains **six distinct subunits (PFD1-PFD6)**, organized as **two alpha-type** and **four beta-type** subunits |
| GO:0051082 unfolded protein binding | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | MODIFY | Summary: unfolded protein binding reviewed for PFD1: MODIFY. Reason: Unfolded protein binding is mechanistically close but too broad; Pfd1 is best represented as a prefoldin protein-folding cochaperone. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin functions largely as an **ATP-independent holdase**, stabilizing folding intermediates and preventing aggregation prior to transfer to CCT/TRiC |
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Download this section (compressed HTML)Q: Which Pfd1-containing prefoldin surfaces distinguish cytoskeletal client capture from the secondary nuclear transcription role?
Q: Does Pfd1 have subunit-specific client preferences within yeast prefoldin beyond the canonical actin and tubulin pathway?
Experiment: Generate Pfd1 separation-of-function mutants at endogenous expression levels and compare actin/tubulin folding, prefoldin complex integrity, chromatin occupancy, and RNA polymerase II elongation phenotypes.
Hypothesis: Pfd1 has separable surfaces for canonical actin/tubulin cochaperone function and non-core transcription-associated function.
Type: separation-of-function mutagenesis
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