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protein_family: Not specified in UniProt
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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P47103
• Protein Description: RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP7; Short=PPIase CYP7; EC=5.2.1.8; AltName: Full=Rotamase CYP7;
• Gene Information: Name=CPR7; OrderedLocusNames=YJR032W; ORFNames=J1585;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Not specified in UniProt
• Key Domains: Cyclophilin-like_dom_sf. (IPR029000); Cyclophilin-type_PPIase_CS. (IPR020892); Cyclophilin-type_PPIase_dom. (IPR002130); TPR-like_helical_dom_sf. (IPR011990); TPR_rpt. (IPR019734)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CPR7" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'CPR7' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene CPR7 (gene ID: CPR7, UniProt: P47103) in yeast.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P47103
• Protein Description: RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP7; Short=PPIase CYP7; EC=5.2.1.8; AltName: Full=Rotamase CYP7;
• Gene Information: Name=CPR7; OrderedLocusNames=YJR032W; ORFNames=J1585;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Not specified in UniProt
• Key Domains: Cyclophilin-like_dom_sf. (IPR029000); Cyclophilin-type_PPIase_CS. (IPR020892); Cyclophilin-type_PPIase_dom. (IPR002130); TPR-like_helical_dom_sf. (IPR011990); TPR_rpt. (IPR019734)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CPR7" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'CPR7' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene CPR7 (gene ID: CPR7, UniProt: P47103) in yeast.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research report: functional annotation of Saccharomyces cerevisiae CPR7 (UniProt P47103, ORF YJR032W)

Executive summary

Saccharomyces cerevisiae CPR7 encodes Cpr7, a cytosolic CyP40-type cyclophilin/immunophilin that functions primarily as a TPR-domain Hsp90 co‑chaperone rather than as a classical standalone prolyl isomerase. Cpr7 contains an N‑terminal cyclophilin (PPIase) domain and a C‑terminal tetratricopeptide repeat (TPR) domain that binds the Hsp90 C‑terminal M/EEVD motif and organizes co‑chaperone/client interactions. Across multiple experimental contexts, the TPR domain is frequently sufficient to rescue key cpr7Δ phenotypes, whereas the PPIase catalytic activity is often dispensable; however, the PPIase domain surface can be required for viability in certain sensitized backgrounds (e.g., cns1 mutants), implying an essential noncatalytic scaffolding function of this domain in Hsp90 machinery organization. (dolinski1998cns1encodesan pages 1-2, tesic2003functionalinteractionsbetween pages 1-1, zuehlke2012chaperoningthechaperone pages 1-2)

1. Key concepts and definitions (current understanding)

1.1 Gene/protein identity verification (critical disambiguation)

Primary yeast literature explicitly identifies CPR7 as one of the two yeast cyclophilin‑40 (CyP40) homologs (CPR6 and CPR7) and analyzes cpr7 deletion phenotypes in the context of the Hsp90 chaperone machine. This matches the UniProt description for P47103 (CPR7/YJR032W) and avoids confusion with similarly named cyclophilins in other organisms. (dolinski1998cns1encodesan pages 1-2, arevalorodriguez2004prolylisomerasesin pages 7-8)

1.2 Protein class: CyP40-type immunophilin

Cyclophilins are peptidyl‑prolyl cis–trans isomerases (PPIases, EC 5.2.1.8) that catalyze isomerization at peptide bonds N‑terminal to proline residues. CyP40-type cyclophilins are distinguished by dual-domain architecture: an N‑terminal cyclophilin/PPIase domain and a C‑terminal TPR region that binds Hsp90. In yeast, Cpr7 conforms to this CyP40 architecture. (dolinski1998cns1encodesan pages 1-2, arevalorodriguez2004prolylisomerasesin pages 7-8, kumar2015hsp90associatedimmunophilinhomolog pages 2-4)

1.3 Domain architecture and Hsp90-binding logic

Cpr7 is described as having an N‑terminal cyclophilin (PPIase) domain followed by ~three TPR motifs (degenerate ~34 aa repeats). Hsp90 binding is mediated by the carboxy‑terminal TPR region, which recognizes the conserved Hsp90 C‑terminal EEVD/MEEVD acceptor motif. A concrete domain boundary used in mechanistic work defined the Cpr7 TPR domain as aa 193–393. (arevalorodriguez2004prolylisomerasesin pages 7-8, zuehlke2012chaperoningthechaperone pages 14-14, zuehlke2012chaperoningthechaperone pages 1-2)

1.4 Enzymatic activity vs. co-chaperone function

Cpr7 has cyclosporin A (CsA)–inhibitable PPIase activity in vitro, consistent with cyclophilins, but multiple genetic and complementation experiments indicate that PPIase catalytic activity is not required for several major in vivo roles (growth rescue, Hsp90 client-related phenotypes, and prion maintenance). Instead, Cpr7’s primary function is best understood as a co-chaperone/scaffold within the Hsp90 network, largely mediated by its TPR domain and noncatalytic surfaces. (arevalorodriguez2004prolylisomerasesin pages 7-8, dolinski1998cns1encodesan pages 1-2, tesic2003functionalinteractionsbetween pages 1-1)

2. Molecular function, pathways, and localization

2.1 Primary molecular function

Primary function (supported): Cpr7 is an Hsp90 co‑chaperone that regulates aspects of the Hsp90 folding cycle and client maturation via its TPR-mediated binding to Hsp90 and interactions with other co-chaperones (notably Cns1 and Sti1). (zuehlke2012chaperoningthechaperone pages 1-2, dolinski1998cns1encodesan pages 1-2, tesic2003functionalinteractionsbetween pages 1-1)

Secondary/biochemical function: Cpr7 is also a PPIase with CsA-inhibitable activity, but the available evidence emphasizes that this enzymatic activity is often not the determinant of cellular phenotypes attributed to Cpr7. (arevalorodriguez2004prolylisomerasesin pages 7-8, kumar2015hsp90associatedimmunophilinhomolog pages 2-4)

2.2 Substrate specificity (PPIase)

The retrieved corpus does not provide a Cpr7-specific peptide substrate preference sequence. The biochemical activity is described at the level of cyclophilin-family chemistry (cis–trans isomerization of X‑Pro peptide bonds) and relative activity compared with Cpr6. (kumar2015hsp90associatedimmunophilinhomolog pages 2-4, arevalorodriguez2004prolylisomerasesin pages 7-8)

2.3 Pathways and interaction partners

Hsp90 chaperone cycle / co-chaperone network: Cpr7 genetically and physically associates with the Hsp90 system. Deletion causes slow growth and hypersensitivity to Hsp90 inhibition, and Cpr7 supports maturation of diverse Hsp90 clients (see below). (dolinski1998cns1encodesan pages 1-2, marsh1998cns1isan pages 1-1, arevalorodriguez2004prolylisomerasesin pages 7-8)

Cns1 (essential TPR co-chaperone): Cns1 was isolated as a high-copy suppressor of the cpr7Δ slow-growth phenotype and is found in complexes with Hsp90 and Cpr7 (but not Cpr6 in the cited experiments). Importantly, CsA inhibited Cpr7–Cns1 interaction but not Cpr7–Hsp90, implying that Cpr7 participates in separable interaction interfaces. (dolinski1998cns1encodesan pages 1-2)

Sti1/Hop: Genetic interaction studies implicate overlapping essential roles for Cpr7 and Sti1 in supporting Hsp90 function and normal growth, consistent with a multi-step cycle in which different TPR co-chaperones bind Hsp90 at different stages. (tesic2003functionalinteractionsbetween pages 1-1, arevalorodriguez2004prolylisomerasesin pages 7-8)

Hsp104 and prion/stress networks: In respiring yeast, the Hsp90 cochaperones Sti1, Cpr7, and Cns1 form complexes with Hsp104 in vivo; Sti1 and Cpr7 can interact with Hsp104 directly in vitro, independent of Hsp90. This supports a shared cochaperone pool linking Hsp90 and Hsp104 systems under specific metabolic conditions. (abbasterki2001hsp104interactswith pages 1-2)

Ribosome / translation link: Cpr7, together with Cpr6 and Cns1, can interact with the intact ribosome, and cpr7 deletion or cns1 mutations confer hygromycin sensitivity, linking the Hsp90 cochaperone network to protein synthesis homeostasis. (tenge2015thehsp90cochaperones pages 1-2)

Chromatin-associated factor Rpd3: Cpr7 was identified in screens for Rpd3 interactors and is reported to interact with Rpd3/Sin3–Rpd3 histone deacetylase components, though the mechanistic relevance to its primary Hsp90 co‑chaperone role is less developed in the retrieved evidence. (arevalorodriguez2004prolylisomerasesin pages 4-6)

2.4 Subcellular localization

A yeast prolyl isomerase review table lists Cpr7 as cytoplasmic, consistent with its role as a cochaperone of cytosolic Hsp90 and its observed interactions with Hsp104 and ribosomes. (arevalorodriguez2004prolylisomerasesin pages 4-6, abbasterki2001hsp104interactswith pages 1-2, tenge2015thehsp90cochaperones pages 1-2)

3. Experimental evidence: phenotypes, domain requirements, and quantitative data

3.1 Growth and Hsp90 inhibitor sensitivity

• cpr7Δ strains are viable but show a slow-growth phenotype. (dolinski1998cns1encodesan pages 1-2, arevalorodriguez2004prolylisomerasesin pages 7-8)
• cpr7 mutants are hypersensitive to geldanamycin, an Hsp90 inhibitor. In Dolinski et al. (1998), assays used 20 mg/mL geldanamycin in plates. (dolinski1998cns1encodesan pages 2-4)

These observations strongly support that Cpr7 supports basal Hsp90-dependent proteostasis. (dolinski1998cns1encodesan pages 1-2)

3.2 Domain dissection: TPR sufficiency and PPIase dispensability

A consistent finding across multiple contexts is that the TPR domain is the key functional module for many cpr7Δ phenotypes:
* Overexpression of the TPR domain alone complements cpr7Δ slow growth and geldanamycin hypersensitivity, whereas the cyclophilin/PPIase domain alone does not. (dolinski1998cns1encodesan pages 1-2, dolinski1998cns1encodesan pages 2-4)
* The isolated Cpr7 TPR domain was defined as aa 193–393 in mechanistic studies. (zuehlke2012chaperoningthechaperone pages 14-14)

However, in sensitized backgrounds, the PPIase domain contributes via noncatalytic functions:
* In cns1 mutant cells, both TPR and the PPIase domain are required for viability, but this requirement does not depend on PPIase catalysis; instead, hydrophilic surface residues on the PPIase domain appear important. (tesic2003functionalinteractionsbetween pages 1-1)

3.3 Hsp90 conformational-cycle regulation (mechanistic model)

Zuehlke & Johnson (2012) provides evidence that Cpr7 regulates the nucleotide-dependent association of Cpr6 with Hsp90, and proposes that Cpr7 promotes proper cycling/release of co-chaperones during the Hsp90 conformational cycle. In a summarized model, absence of Cpr7 leads to persistent Hsp82–Cpr6 complexes after ATP hydrolysis. (zuehlke2012chaperoningthechaperone pages 1-2, zuehlke2012chaperoningthechaperone pages 8-9)

3.4 Hsp90 client proteins and pathways

Cpr7 is required for maximal function of several Hsp90-dependent clients and pathways, including:
* Glucocorticoid receptor (GR) activity/maturation in yeast reporter assays; CNS1 overexpression in cpr7Δ largely restored GR activity. (marsh1998cns1isan pages 1-1)
* pp60v-src (v-Src) maximal activity; Cpr7 is required for maximal activity of this heterologous Hsp90 client. (marsh1998cns1isan pages 1-1)
* Heat shock transcription factor (HSF) negative regulation; HSF activity is derepressed in cpr7Δ, and Cns1 overexpression restores negative regulation in cpr7Δ. (arevalorodriguez2004prolylisomerasesin pages 7-8, marsh1998cns1isan pages 1-1)
* Mal63 (maltose-regulon transcriptional activator) stability: Mal63 half-life is shortened in compromised Hsp90+Cpr7 backgrounds (reported in the review synthesis). (arevalorodriguez2004prolylisomerasesin pages 7-8)

3.5 Prion biology: [URE3] stability

Kumar et al. (2015) shows a strong, quantitative phenotype:
* Deletion of CPR7 causes >99% loss of [URE3] propagation (cells become [ure‑o]). (kumar2015hsp90associatedimmunophilinhomolog pages 7-10)
* This effect is strongly dependent on the TPR domain (domain-swapping constructs bearing the Cpr7 TPR support [URE3]). (kumar2015hsp90associatedimmunophilinhomolog pages 7-10)
* A Cpr7 derivative lacking the PPIase domain still supports stable [URE3], supporting that PPIase activity is dispensable for this function. (kumar2015hsp90associatedimmunophilinhomolog pages 7-10)
* As a comparator, Ssa1 overexpression destabilized [URE3] only modestly (7–8% [ure‑o]), arguing Cpr7 loss is not explained solely by elevated Hsp70. (kumar2015hsp90associatedimmunophilinhomolog pages 7-10)

3.6 Ribosome/translation phenotypes

Cpr7 (with Cpr6 and Cns1) interacts with the intact ribosome, and loss of CPR7 or mutations in CNS1 confer hygromycin sensitivity, linking the Hsp90 cochaperone network to translation quality control. (tenge2015thehsp90cochaperones pages 1-2)

4. Recent developments (prioritizing 2023–2024)

4.1 2024: Cpr7/Cns1 in eEF2 proteostasis

A 2024 PLOS Genetics study situates Cpr7 in a modern, client-specific proteostasis circuit centered on translation elongation factor 2 (eEF2):
* The paper notes that a physical and genetic network consisting of Cpr7 and Cns1 had been recognized for years, but more recently these cochaperones (with Hgh1) were shown to regulate eEF2 folding/solubility. (fulton2024hsp90andcochaperones pages 4-5)
* In their experiments, deletion of CPR7 (and mutation of CNS1) resulted in significantly lower levels of soluble His‑eEF2 recovered by Ni-resin and lower eEF2 levels in lysates, consistent with decreased stability/solubility. (fulton2024hsp90andcochaperones pages 4-5)
* They cite prior quantitative estimates from earlier work: after CPR7 deletion or CNS1 knockdown, about 20% of eEF2 remained soluble, while after HGH1 deletion, about 40% remained soluble. (fulton2024hsp90andcochaperones pages 4-5)

These data extend CPR7 annotation from “general Hsp90 co-chaperone” into a defined translation-related client pathway (eEF2 proteostasis). (fulton2024hsp90andcochaperones pages 4-5)

4.2 2023–2024: current expert frameworks for yeast Hsp90/co-chaperone biology

Recent Hsp90 literature in yeast emphasizes cochaperones as regulators of progression through distinct conformational stages of the Hsp90 cycle, affecting client fate and drug sensitivity (e.g., NVP-AUY922/luminespib sensitivity correlated with defects in conformational steps). While these mechanistic papers focus heavily on Hsp90 mutants and other cochaperones, they reinforce the conceptual basis for why TPR cochaperones such as Cpr7 can have strong client-specific effects. (mercier2023hsp90mutantswith pages 1-2, mercier2023hsp90mutantswith pages 2-4, rios2024insightsintohsp90 pages 3-5)

5. Current applications and real-world implementations

5.1 Yeast as a platform to dissect Hsp90/co-chaperone function and drug responses

CPR7’s most direct “real-world” relevance is as part of the yeast Hsp90 machinery used for:
* Mechanistic dissection of chaperone cycles using genetics and defined clients (e.g., GR and v-Src reporters) (marsh1998cns1isan pages 1-1, tesic2003functionalinteractionsbetween pages 1-1)
* Chemical biology screens and sensitivity assays with Hsp90 inhibitors (e.g., geldanamycin hypersensitivity in cpr7 mutants) to understand pathway buffering and co-chaperone contributions. (dolinski1998cns1encodesan pages 2-4)

Because Cpr7 influences the maturation of heterologous clients and drug sensitivity, CPR7 status can be used to tune or interpret Hsp90-inhibitor phenotypes in yeast models, including those relevant to oncology drug discovery pipelines where Hsp90 is a target. (mercier2023hsp90mutantswith pages 1-2, dolinski1998cns1encodesan pages 2-4)

5.2 Applications to prion biology and translation quality control

The strong penetrance of [URE3] loss in cpr7Δ provides a genetic entry point for studying prion propagation mechanisms and the role of the Hsp90/co-chaperone network in epigenetic protein-based inheritance. (kumar2015hsp90associatedimmunophilinhomolog pages 7-10)

Similarly, ribosome interaction and hygromycin sensitivity connect Cpr7 to translation-linked proteostasis, relevant to understanding how chaperone systems couple to protein synthesis. (tenge2015thehsp90cochaperones pages 1-2)

6. Expert interpretation and synthesis (authoritative analysis)

1. Cpr7 is best annotated as an Hsp90 co-chaperone with immunophilin architecture. While it is enzymatically a PPIase, multiple phenotypes map primarily to its TPR/Hsp90-binding function and noncatalytic domain surfaces. (dolinski1998cns1encodesan pages 1-2, tesic2003functionalinteractionsbetween pages 1-1, zuehlke2012chaperoningthechaperone pages 1-2)

2. Catalysis-independent functions are central. The repeated observation that the PPIase domain can be deleted without abolishing growth/Hsp90 activity in some assays, and that prion maintenance depends on TPR, suggests Cpr7 has evolved primarily as a scaffold/adaptor in the Hsp90 network rather than as a general proline isomerase acting on bulk substrates. (kumar2015hsp90associatedimmunophilinhomolog pages 2-4, kumar2015hsp90associatedimmunophilinhomolog pages 7-10)

3. Cpr7 has client- and context-specific roles. Cpr7 supports maturation of multiple clients (GR, v-Src, HSF regulation), affects prion propagation ([URE3]), and participates in translation proteostasis (ribosome interaction; eEF2 folding), indicating that Hsp90 co-chaperones partition Hsp90 capacity into selective modules. (marsh1998cns1isan pages 1-1, kumar2015hsp90associatedimmunophilinhomolog pages 7-10, tenge2015thehsp90cochaperones pages 1-2, fulton2024hsp90andcochaperones pages 4-5)

7. Evidence map (summary table)

The following table consolidates key findings, quantitative details, and DOI URLs.

Table: This table summarizes experimentally supported features of Saccharomyces cerevisiae Cpr7, including its domain architecture, major interaction partners, Hsp90-related functions, and distinctive mutant phenotypes. It is useful as a compact evidence map linking specific findings to methods, quantitative details, and source papers.

References (URLs and dates highlighted)

• Dolinski KJ, Cardenas ME, Heitman J. 1998-12. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.18.12.7344 (dolinski1998cns1encodesan pages 1-2, dolinski1998cns1encodesan pages 2-4)
• Marsh JA, Kalton HM, Gaber RF. 1998-12. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.18.12.7353 (marsh1998cns1isan pages 1-1)
• Abbas-Terki T, Donzé O, Briand P-A, Picard D. 2001-11. Molecular and Cellular Biology. https://doi.org/10.1128/MCB.21.22.7569-7575.2001 (abbasterki2001hsp104interactswith pages 1-2)
• Tesic M, Marsh JA, Cullinan SB, Gaber RF. 2003-08. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m304315200 (tesic2003functionalinteractionsbetween pages 1-1, tesic2003functionalinteractionsbetween pages 4-5)
• Arévalo-Rodríguez M, Wu X, Hanes S, Heitman J. 2004-09. Frontiers in Bioscience. https://doi.org/10.2741/1405 (arevalorodriguez2004prolylisomerasesin pages 4-6, arevalorodriguez2004prolylisomerasesin pages 7-8)
• Zuehlke AD, Johnson JL. 2012-07. Genetics. https://doi.org/10.1534/genetics.112.140319 (zuehlke2012chaperoningthechaperone pages 1-2, zuehlke2012chaperoningthechaperone pages 8-9)
• Zuehlke AD, Wren N, Tenge V, Johnson JL. 2013-09. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m113.504142 (zuehlke2013interactionofheat pages 1-1)
• Tenge VR, Zuehlke AD, Shrestha N, Johnson JL. 2015-01. Eukaryotic Cell. https://doi.org/10.1128/ec.00170-14 (tenge2015thehsp90cochaperones pages 1-2)
• Kumar N, Gaur D, Gupta A, et al. 2015-10. PLOS Genetics. https://doi.org/10.1371/journal.pgen.1005567 (kumar2015hsp90associatedimmunophilinhomolog pages 7-10)
• Mercier R, Yama D, LaPointe P, Johnson JL. 2023-05-25. PLOS Genetics. https://doi.org/10.1371/journal.pgen.1010772 (mercier2023hsp90mutantswith pages 1-2, mercier2023hsp90mutantswith pages 2-4)
• Rios EI, Hunsberger IL, Johnson JL. 2024-02. Frontiers in Molecular Biosciences. https://doi.org/10.3389/fmolb.2024.1325590 (rios2024insightsintohsp90 pages 3-5)
• Fulton MD, Yama DJ, Dahl E, Johnson JL. 2024-12-09. PLOS Genetics. https://doi.org/10.1371/journal.pgen.1011508 (fulton2024hsp90andcochaperones pages 4-5)

Scope and limitations

This report is strictly limited to the verified yeast CPR7/P47103/YJR032W protein. Within the retrieved corpus, Cpr7-specific enzymatic kinetic constants (e.g., kcat/KM, Ki for CsA for Cpr7 itself) and high-resolution localization microscopy were not available; claims about catalytic parameters and localization were therefore restricted to what is explicitly reported (comparative enzymology vs Cpr6; cytoplasmic localization as summarized in a yeast PPIase review). (arevalorodriguez2004prolylisomerasesin pages 7-8, arevalorodriguez2004prolylisomerasesin pages 4-6)

References

1. (dolinski1998cns1encodesan pages 1-2): Kara J. Dolinski, Maria E. Cardenas, and Joseph Heitman. Cns1 encodes an essential p60/sti1 homolog in saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with hsp90. Molecular and Cellular Biology, 18:7344-7352, Dec 1998. URL: https://doi.org/10.1128/mcb.18.12.7344, doi:10.1128/mcb.18.12.7344. This article has 122 citations and is from a domain leading peer-reviewed journal.

2. (tesic2003functionalinteractionsbetween pages 1-1): Marija Tesic, James A. Marsh, Sara B. Cullinan, and Richard F. Gaber. Functional interactions between hsp90 and the co-chaperones cns1 and cpr7 in saccharomyces cerevisiae*. Journal of Biological Chemistry, 278:32692-32701, Aug 2003. URL: https://doi.org/10.1074/jbc.m304315200, doi:10.1074/jbc.m304315200. This article has 69 citations and is from a domain leading peer-reviewed journal.

3. (zuehlke2012chaperoningthechaperone pages 1-2): Abbey D Zuehlke and Jill L Johnson. Chaperoning the chaperone: a role for the co-chaperone cpr7 in modulating hsp90 function in saccharomyces cerevisiae. Genetics, 191:805-814, Jul 2012. URL: https://doi.org/10.1534/genetics.112.140319, doi:10.1534/genetics.112.140319. This article has 45 citations and is from a domain leading peer-reviewed journal.

4. (arevalorodriguez2004prolylisomerasesin pages 7-8): M. Arévalo-Rodríguez, Xiaoyun Wu, S. Hanes, and J. Heitman. Prolyl isomerases in yeast. Frontiers in bioscience : a journal and virtual library, 9:2420-46, Sep 2004. URL: https://doi.org/10.2741/1405, doi:10.2741/1405. This article has 151 citations.

5. (kumar2015hsp90associatedimmunophilinhomolog pages 2-4): Navinder Kumar, Deepika Gaur, Arpit Gupta, Anuradhika Puri, D. Sharma, and T. Serio. Hsp90-associated immunophilin homolog cpr7 is required for the mitotic stability of [ure3] prion in saccharomyces cerevisiae. PLOS Genetics, 11:e1005567, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005567, doi:10.1371/journal.pgen.1005567. This article has 31 citations and is from a domain leading peer-reviewed journal.

6. (zuehlke2012chaperoningthechaperone pages 14-14): Abbey D Zuehlke and Jill L Johnson. Chaperoning the chaperone: a role for the co-chaperone cpr7 in modulating hsp90 function in saccharomyces cerevisiae. Genetics, 191:805-814, Jul 2012. URL: https://doi.org/10.1534/genetics.112.140319, doi:10.1534/genetics.112.140319. This article has 45 citations and is from a domain leading peer-reviewed journal.

7. (marsh1998cns1isan pages 1-1): James A. Marsh, Helen M. Kalton, and Richard F. Gaber. Cns1 is an essential protein associated with the hsp90 chaperone complex in saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7δcells. Molecular and Cellular Biology, 18:7353-7359, Dec 1998. URL: https://doi.org/10.1128/mcb.18.12.7353, doi:10.1128/mcb.18.12.7353. This article has 105 citations and is from a domain leading peer-reviewed journal.

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9. (tenge2015thehsp90cochaperones pages 1-2): Victoria R. Tenge, Abbey D. Zuehlke, Neelima Shrestha, and Jill L. Johnson. The hsp90 cochaperones cpr6, cpr7, and cns1 interact with the intact ribosome. Eukaryotic Cell, 14:55-63, Jan 2015. URL: https://doi.org/10.1128/ec.00170-14, doi:10.1128/ec.00170-14. This article has 23 citations and is from a peer-reviewed journal.

10. (arevalorodriguez2004prolylisomerasesin pages 4-6): M. Arévalo-Rodríguez, Xiaoyun Wu, S. Hanes, and J. Heitman. Prolyl isomerases in yeast. Frontiers in bioscience : a journal and virtual library, 9:2420-46, Sep 2004. URL: https://doi.org/10.2741/1405, doi:10.2741/1405. This article has 151 citations.

11. (dolinski1998cns1encodesan pages 2-4): Kara J. Dolinski, Maria E. Cardenas, and Joseph Heitman. Cns1 encodes an essential p60/sti1 homolog in saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with hsp90. Molecular and Cellular Biology, 18:7344-7352, Dec 1998. URL: https://doi.org/10.1128/mcb.18.12.7344, doi:10.1128/mcb.18.12.7344. This article has 122 citations and is from a domain leading peer-reviewed journal.

12. (zuehlke2012chaperoningthechaperone pages 8-9): Abbey D Zuehlke and Jill L Johnson. Chaperoning the chaperone: a role for the co-chaperone cpr7 in modulating hsp90 function in saccharomyces cerevisiae. Genetics, 191:805-814, Jul 2012. URL: https://doi.org/10.1534/genetics.112.140319, doi:10.1534/genetics.112.140319. This article has 45 citations and is from a domain leading peer-reviewed journal.

13. (kumar2015hsp90associatedimmunophilinhomolog pages 7-10): Navinder Kumar, Deepika Gaur, Arpit Gupta, Anuradhika Puri, D. Sharma, and T. Serio. Hsp90-associated immunophilin homolog cpr7 is required for the mitotic stability of [ure3] prion in saccharomyces cerevisiae. PLOS Genetics, 11:e1005567, Oct 2015. URL: https://doi.org/10.1371/journal.pgen.1005567, doi:10.1371/journal.pgen.1005567. This article has 31 citations and is from a domain leading peer-reviewed journal.

14. (fulton2024hsp90andcochaperones pages 4-5): Melody D. Fulton, Danielle J. Yama, Ella Dahl, and Jill L. Johnson. Hsp90 and cochaperones have two genetically distinct roles in regulating eef2 function. PLOS Genetics, 20:e1011508, Dec 2024. URL: https://doi.org/10.1371/journal.pgen.1011508, doi:10.1371/journal.pgen.1011508. This article has 5 citations and is from a domain leading peer-reviewed journal.

15. (mercier2023hsp90mutantswith pages 1-2): Rebecca Mercier, Danielle Yama, Paul LaPointe, and Jill L. Johnson. Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle. PLOS Genetics, 19:e1010772, May 2023. URL: https://doi.org/10.1371/journal.pgen.1010772, doi:10.1371/journal.pgen.1010772. This article has 13 citations and is from a domain leading peer-reviewed journal.

16. (mercier2023hsp90mutantswith pages 2-4): Rebecca Mercier, Danielle Yama, Paul LaPointe, and Jill L. Johnson. Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle. PLOS Genetics, 19:e1010772, May 2023. URL: https://doi.org/10.1371/journal.pgen.1010772, doi:10.1371/journal.pgen.1010772. This article has 13 citations and is from a domain leading peer-reviewed journal.

17. (rios2024insightsintohsp90 pages 3-5): Erick I. Rios, Isabel L. Hunsberger, and Jill L. Johnson. Insights into hsp90 mechanism and in vivo functions learned from studies in the yeast, saccharomyces cerevisiae. Frontiers in Molecular Biosciences, Feb 2024. URL: https://doi.org/10.3389/fmolb.2024.1325590, doi:10.3389/fmolb.2024.1325590. This article has 8 citations.

18. (tesic2003functionalinteractionsbetween pages 4-5): Marija Tesic, James A. Marsh, Sara B. Cullinan, and Richard F. Gaber. Functional interactions between hsp90 and the co-chaperones cns1 and cpr7 in saccharomyces cerevisiae*. Journal of Biological Chemistry, 278:32692-32701, Aug 2003. URL: https://doi.org/10.1074/jbc.m304315200, doi:10.1074/jbc.m304315200. This article has 69 citations and is from a domain leading peer-reviewed journal.

19. (zuehlke2013interactionofheat pages 1-1): Abbey D. Zuehlke, Nicholas Wren, Victoria Tenge, and Jill L. Johnson. Interaction of heat shock protein 90 and the co-chaperone cpr6 with ura2, a bifunctional enzyme required for pyrimidine biosynthesis. Journal of Biological Chemistry, 288:27406-27414, Sep 2013. URL: https://doi.org/10.1074/jbc.m113.504142, doi:10.1074/jbc.m113.504142. This article has 15 citations and is from a domain leading peer-reviewed journal.

Citations

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9. URE3
10. ure‑o
11. ure-o
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