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gene_info: Name=CCT6; Synonyms=TCP20, TCP6; OrderedLocusNames=YDR188W; ORFNames=YD9395.21;
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protein_family: Belongs to the TCP-1 chaperonin family. .
protein_domains: Chap_CCT_zeta. (IPR012722); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS.
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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: P39079
• Protein Description: RecName: Full=T-complex protein 1 subunit zeta; Short=TCP-1-zeta; AltName: Full=CCT-zeta;
• Gene Information: Name=CCT6; Synonyms=TCP20, TCP6; OrderedLocusNames=YDR188W; ORFNames=YD9395.21;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_zeta. (IPR012722); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS. (IPR002194); Cpn60/GroEL/TCP-1. (IPR002423); GroEL-like_apical_dom_sf. (IPR027409)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CCT6" 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 'CCT6' 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 CCT6 (gene ID: CCT6, UniProt: P39079) 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: P39079
• Protein Description: RecName: Full=T-complex protein 1 subunit zeta; Short=TCP-1-zeta; AltName: Full=CCT-zeta;
• Gene Information: Name=CCT6; Synonyms=TCP20, TCP6; OrderedLocusNames=YDR188W; ORFNames=YD9395.21;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_zeta. (IPR012722); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS. (IPR002194); Cpn60/GroEL/TCP-1. (IPR002423); GroEL-like_apical_dom_sf. (IPR027409)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CCT6" 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 'CCT6' 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 CCT6 (gene ID: CCT6, UniProt: P39079) 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: CCT6 (YDR188W; UniProt P39079) in Saccharomyces cerevisiae (S288c)

Executive summary

CCT6 (YDR188W; UniProt P39079) encodes T-complex protein 1 subunit zeta (Cct6p; also called CCT-ζ), one of eight paralogous subunits that assemble into the essential cytosolic group II chaperonin TRiC/CCT. TRiC/CCT is a ~1 MDa ATP-dependent double-ring folding machine required for maturation of a specific subset of eukaryotic proteins—classically actin and tubulin—and is estimated to mediate folding of roughly ~10% of newly synthesized polypeptides in yeast. Yeast genetics further indicates that CCT6 is essential, and that excess/unassembled Cct6p (produced by overexpression) can suppress multiple conditional growth defects in otherwise unrelated pathways (TOR signaling, trafficking/vacuole/cell wall, ubiquitin ligase function), implying physiologically meaningful activity beyond (or in addition to) the assembled TRiC complex. Recent 2023–2024 studies refine TRiC allostery/ATPase kinetics, connect TRiC malfunction to stress-response pathways (e.g., cell-wall integrity MAPK signaling), and expand the functional landscape to include nuclear roles for TRiC in transcriptional homeostasis; however, these advances are mostly complex-level and not uniquely CCT6-subunit–specific. (grantham2020themolecularchaperone pages 1-2, dube2023saccharomycescerevisiaesurvival pages 1-4, kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4)

Evidence map (high-level)

Table: This table summarizes experimentally supported functional annotation evidence for yeast CCT6/YDR188W/P39079, emphasizing identity verification, complex role, subunit specialization, genetics, localization, and 2023-2024 developments. It is useful as a compact evidence map for building a narrative report while keeping organism-specific claims separate from broader TRiC/CCT findings.

1) Gene/protein identity verification (disambiguation)

The target is yeast CCT6 (ordered locus name YDR188W; UniProt P39079), a TRiC/CCT subunit (Cct6p). Yeast-focused primary literature explicitly treats CCT6 as a chaperonin subunit gene and performs yeast genetics with cct6 alleles and CCT6 overexpression constructs, consistent with the UniProt record and domain/family assignment (TCP-1 chaperonin family). (kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4)

2) Key concepts and definitions (current understanding)

2.1 TRiC/CCT as a eukaryotic group II chaperonin

TRiC/CCT (TCP-1 Ring Complex / Chaperonin Containing TCP-1) is an essential eukaryotic chaperonin that forms two stacked rings, each ring containing eight different subunits (CCT1–CCT8) in a fixed arrangement, producing a central chamber where folding can proceed under “caged” conditions coupled to an ATP-driven conformational cycle. (grantham2020themolecularchaperone pages 1-2, gvozdenov2024triccctchaperoningoverns pages 1-6)

2.2 Substrate spectrum and “primary function” framing for CCT6

For functional annotation, the most defensible “primary function” for CCT6 is: a structural/ATPase subunit of the TRiC/CCT chaperonin that contributes to ATP-dependent folding and maturation of obligate cytosolic substrates, especially actin and tubulin, and other topologically complex clients. Reviews emphasize that actin and tubulin are core/obligate CCT substrates, and TRiC also contributes to assembly of select multiprotein complexes (e.g., VHL–Elongin) and interacts with regulators (e.g., gelsolin) in a non-classical chaperoning mode. (grantham2020themolecularchaperone pages 1-2, willison2018thestructureand pages 1-2)

2.3 Subunit specialization within TRiC/CCT

Unlike bacterial GroEL (homooligomer), TRiC is heterooligomeric, allowing subunit-specific substrate contacts and asymmetric ATPase/allosteric behavior. Experimental and structural analyses (summarized in yeast TRiC-focused work) group subunits into two “hemispheres” with differing nucleotide affinity and ATPase roles. CCT6 is consistently placed in the low ATP-affinity hemisphere (with CCT3/6/7/8), with sequence divergence near the nucleotide pocket proposed to reduce nucleotide exchange/ATP binding; yeast mutational data indicate that ATPase/P-loop disruption is more deleterious in high-affinity subunits than in low-affinity ones. (kelly2020structuralandfunctionala pages 42-48, kelly2020structuralandfunctional pages 42-48)

3) Molecular/structural annotation of yeast Cct6p

3.1 Subunit position in the yeast TRiC/CCT ring

A yeast internal-subunit eGFP labeling strategy combined with cryo-EM (YISEL) enabled unambiguous subunit assignment in yeast TRiC, including CCT6. This work assigns CCT6 as an on-axis subunit and places it at a defined position in the ring architecture (Figure evidence). (zang2018developmentofa pages 1-2, zang2018developmentofa media 20a150a9)

3.2 Structural role during ring closure and inter-ring communication

Structural analyses summarized for yeast TRiC indicate that the N-terminus of CCT6 participates in an inter-ring interaction network during closure, stacking with the trans ring alongside other low-affinity hemisphere subunits. This supports the view that CCT6 contributes importantly to mechanical/structural coupling of the two rings through the ATP-driven cycle, even if its own ATPase contribution is reduced relative to high-affinity subunits. (kelly2020structuralandfunctionala pages 42-48, kelly2020structuralandfunctional pages 42-48)

4) Cellular localization and where Cct6p acts

4.1 Canonical localization: cytosolic proteostasis

TRiC/CCT is classically considered a cytosolic folding machine that supports co-/post-translational maturation of a substantial fraction of the proteome. Yeast-focused work explicitly reiterates TRiC/CCT as a cytosolic cylindrical complex encoded by eight essential genes and contributing to folding of ~10% of yeast cellular polypeptides. (dube2023saccharomycescerevisiaesurvival pages 1-4)

4.2 Emerging localization/function: nuclear TRiC/CCT

A 2024 preprint reports TRiC/CCT is present in the nucleus and proposes a direct role in regulating RNA polymerase II activity and nascent RNA production (with effects persisting when TRiC is restricted to the cytoplasm, supporting a direct nuclear role in their model). This expands likely functional contexts for all TRiC subunits (including CCT6), although it does not isolate a CCT6-specific nuclear mechanism. (gvozdenov2024triccctchaperoningoverns pages 1-6)

5) Yeast genetics: essentiality, phenotypes, and CCT6-specific functional inferences

5.1 Essentiality

Yeast gene disruption experiments and genetic summaries state that all eight CCT genes (CCT1–CCT8) are essential, which includes CCT6. (kabir2008overexpressedribosomalproteins pages 1-2, kabir2005physiologicaleffectsof pages 2-4)

5.2 Conditional alleles and cytoskeleton-linked phenotypes

A panel of temperature-sensitive cct6 alleles has been described (e.g., cct6-14, -18, -27, -74, -85, -93, -97). Reported phenotypes include TBZ sensitivity (consistent with microtubule-associated stress) and in some alleles NaCl sensitivity (often used as an actin/cytoskeleton stress readout in these legacy screens). (kabir2008overexpressedribosomalproteins pages 1-2, kabir2008overexpressedribosomalproteins pages 2-3)

5.3 Multicopy suppression: unassembled Cct6p as a functional entity

A central yeast-specific insight is that overexpression of CCT6 can suppress diverse conditional phenotypes, including defects caused by tor2-21, lst8-2, rsp5-9, and growth inhibition caused by concomitant overexpression of Sit4p and Sap155p. Importantly, fractionation/abundance analysis indicates that overexpressing CCT6 increases the level of unassociated (unassembled) Cct6p, while the assembled TRiC/CCT complex remains at normal levels—supporting a model where unassembled Cct6p has physiological effects (e.g., substrate sequestration/competition for modifying activities) beyond simply boosting holo-complex abundance. (kabir2005physiologicaleffectsof pages 1-2, kabir2005physiologicaleffectsof pages 2-4)

5.4 Separation-of-function: ATP-binding motif required for suppression but not viability

Kabir et al. examined many altered forms of Cct6p and report that a CCT6 allele with GDGTT→AAAAA substitutions in the conserved ATP-binding motif (cct6-24) is unable to suppress the above traits, yet is functional for growth. This strongly supports that (i) Cct6p has separable functional states and (ii) suppression by unassembled Cct6p likely requires a specific ATP-associated conformation or activity. (kabir2005physiologicaleffectsof pages 1-2)

5.5 Proteome-scale phenotyping distinguishes CCT6 from other subunits

High-throughput microscopy profiling comparing ATP-site mutants in different TRiC subunits found that CCT subunits can have distinguishable in vivo consequences; in particular, the study emphasizes that the CCT3 mutant showed stronger associations with Q/N-rich proteins and P-body phenotypes than the CCT6 mutant, consistent with subunit-specific substrate/interactome specialization. (nadlerholly2012interactionsofsubunit pages 1-2)

6) Pathways and biological processes linked to CCT6/TRiC in yeast

6.1 TOR signaling / actin polarization axis

Overexpression of CCT6 suppresses tor2-21 conditional phenotypes and is linked to partial restoration of actin cytoskeleton polarization in that genetic background, tying TRiC/CCT (and/or unassembled Cct6p) to a TOR2-dependent actin organization pathway. (kabir2005physiologicaleffectsof pages 2-4)

6.2 Trafficking/cell wall integrity and ubiquitin ligase connections

CCT6 overexpression suppresses phenotypes of lst8-2 (a TOR-associated factor required for sorting of diverse proteins at the Golgi and associated with cell wall integrity) and rsp5-9 (an essential ubiquitin–protein ligase with broad roles including endocytosis and actin dynamics). These suppression relationships suggest that TRiC/CCT proteostasis capacity and/or Cct6p-mediated sequestration can buffer defects in trafficking, membrane protein turnover, and cell surface/cell wall regulation. (kabir2005physiologicaleffectsof pages 2-4)

6.3 Stress physiology and the cell wall integrity MAPK pathway (recent)

A 2023 yeast study using a folding-defective cct7 mutant reports temperature and cell-wall-stressor sensitivity and rescue by overexpression of PKC1 and SLT2 (MAPK cell wall integrity pathway components), supporting a functional interface between TRiC/CCT-dependent folding and cell-wall integrity signaling under heat stress. While not CCT6-specific, it is relevant to interpreting downstream consequences of impaired TRiC activity in yeast and potential contexts where CCT6 alleles may manifest. (dube2023saccharomycescerevisiaesurvival pages 1-4)

7) Recent developments (prioritizing 2023–2024)

7.1 Quantitative TRiC kinetics in yeast (2023)

A 2023 study analyzing yeast TRiC with disease-associated mutations in CCT2 quantified ATPase behavior and reported apparent ATP binding constants and turnover (e.g., WT K1 ~8.3 μM, K2 ~110 μM; kcat ~0.043–0.053 s−1 under their fitted model) and showed that a double mutation reduces ADP off-rate, stabilizing closed states. This strengthens the mechanistic framework in which different subunits contribute differently to allosteric cycling—contextually relevant to CCT6 as a low-affinity hemisphere member—even though the mutation is in CCT2 rather than CCT6. (roy2023reducedadpoffrate pages 1-2, kelly2020structuralandfunctional pages 42-48)

7.2 TRiC cochaperone cooperation and CCT6 contact surfaces (2024)

A 2024 cryo-EM/XL-MS study of TRiC cooperation with PhLP2A (phosducin-like protein) in the folding cycle reports that in the presence of substrate, actin and PhLP2A segregate into opposing chambers, each binding positively charged inner surface residues from CCT1/3/6/8. This provides modern structural evidence that CCT6 contributes directly to the physicochemical environment and binding surfaces engaged during actin folding intermediates. (junsun2024astructuralvista pages 1-2)

7.3 Nuclear TRiC and transcriptional homeostasis in yeast (2024 preprint)

A 2024 yeast study proposes TRiC/CCT has a direct nuclear role modulating RNA polymerase II activity and nascent RNA output, suggesting TRiC contributes to cell homeostasis beyond canonical cytosolic folding. This is a notable expansion of functional annotation scope for the complex and likely relevant to CCT6 as a subunit, but remains preprint-stage and not subunit-resolved. (gvozdenov2024triccctchaperoningoverns pages 1-6)

8) Current applications and real-world implementations

8.1 Yeast as a functional-genomics platform to probe chaperonin subunits

CCT6 is used experimentally as (i) a genetically essential proteostasis component (ts alleles) and (ii) a multicopy suppressor whose overexpression reveals buffering relationships across major pathways (TOR signaling, trafficking/cell wall, ubiquitin-mediated regulation). This makes CCT6 a practical tool for dissecting genetic robustness and proteostasis-pathway crosstalk in an industrially and medically relevant model organism. (kabir2005physiologicaleffectsof pages 1-2, kabir2008overexpressedribosomalproteins pages 2-3)

8.2 Structural biology and engineering of macromolecular machines

The YISEL internal labeling method demonstrated in yeast TRiC enables precise subunit assignment in challenging hetero-oligomeric complexes and is itself an implementation with broader utility for macromolecular complex annotation and cryo-EM mapping—directly leveraging yeast CCT6 subunit labeling/assignment. (zang2018developmentofa pages 1-2, zang2018developmentofa media 20a150a9)

8.3 Disease analogy and mechanistic transfer (caveated)

While human disease phenotypes are not part of yeast CCT6 annotation per se, yeast TRiC studies (e.g., kinetic analysis of disease-linked CCT2 mutations) illustrate how yeast TRiC serves as a mechanistic model for conserved chaperonin function and allosteric defects. Any extension to CCT6-related human disease or therapeutic targeting should be made cautiously and requires direct evidence not provided here. (roy2023reducedadpoffrate pages 1-2)

9) Relevant statistics and quantitative data (from retrieved sources)

• Essential genes: CCT1–CCT8 are essential in yeast. (kabir2008overexpressedribosomalproteins pages 1-2, kabir2005physiologicaleffectsof pages 2-4)
• Proteostasis workload estimate: TRiC/CCT contributes to folding of ~10% of yeast cellular polypeptides (as stated in yeast stress study background). (dube2023saccharomycescerevisiaesurvival pages 1-4)
• Suppression screen scale: 22 multicopy suppressors were isolated for a cct4 ts allele; 14 encoded ribosomal proteins; some suppressors also acted on cct6 alleles. (kabir2008overexpressedribosomalproteins pages 1-2, kabir2008overexpressedribosomalproteins pages 2-3)
• TRiC ATPase kinetics (yeast, WT): apparent ATP binding constants (K1 ~8.3 μM, K2 ~110 μM) and turnover (kcat ~0.043–0.053 s−1) reported in one fitted model/condition set. (roy2023reducedadpoffrate pages 1-2)

10) Expert interpretation and limitations

1. Most CCT6-specific “function” evidence in yeast is genetic (essentiality; ts alleles; multicopy suppression; separation-of-function for suppression vs viability), while client specificity is more firmly established at the TRiC complex level (actin/tubulin and select other classes). Therefore, the most accurate functional annotation for CCT6 is as a TRiC/CCT subunit that supports folding of obligate cytosolic substrates and TRiC conformational cycling, with additional evidence that unassembled Cct6p can modulate cell physiology in an ATP-motif–dependent manner. (kabir2005physiologicaleffectsof pages 1-2, grantham2020themolecularchaperone pages 1-2)
2. Recent 2023–2024 research largely refines TRiC mechanism, stress crosstalk, and nuclear roles, but is not yet fully subunit-resolved for CCT6 in yeast. The strongest 2024 subunit-level mechanistic link involving CCT6 is structural evidence that CCT6 contributes inner-surface residues contacted in the actin/PhLP2A folding context. (junsun2024astructuralvista pages 1-2)

Key cited sources (with dates and URLs)

• Kabir MA et al. Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast. Feb 2005. https://doi.org/10.1002/yea.1210 (kabir2005physiologicaleffectsof pages 1-2)
• Kabir MA & Sherman F. Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae. FEMS Yeast Research. Dec 2008. https://doi.org/10.1111/j.1567-1364.2008.00425.x (kabir2008overexpressedribosomalproteins pages 1-2)
• Zang Y et al. Development of a yeast internal-subunit eGFP labeling strategy… TRiC/CCT. Scientific Reports. Feb 2018. https://doi.org/10.1038/s41598-017-18962-y (zang2018developmentofa pages 1-2)
• Willison KR. The structure and evolution of eukaryotic chaperonin-containing TCP-1… folds actin. Biochemical Journal. Oct 2018. https://doi.org/10.1042/BCJ20170378 (willison2018thestructureand pages 1-2)
• Grantham J. The Molecular Chaperone CCT/TRiC… Frontiers in Genetics. Mar 2020. https://doi.org/10.3389/fgene.2020.00172 (grantham2020themolecularchaperone pages 1-2)
• Roy M et al. Reduced ADP off-rate… yeast CCT2 double mutation… Communications Biology. Aug 2023. https://doi.org/10.1038/s42003-023-05261-8 (roy2023reducedadpoffrate pages 1-2)
• Dube A et al. S. cerevisiae survival against heat stress entails… CCT and cell wall integrity pathway. Biologia Futura. Nov 2023. https://doi.org/10.1007/s42977-023-00192-1 (dube2023saccharomycescerevisiaesurvival pages 1-4)
• Park J et al. A structural vista of PhLP2A–TRiC cooperation… Nature Communications. Feb 2024. https://doi.org/10.1038/s41467-024-45242-x (junsun2024astructuralvista pages 1-2)
• Gvozdenov Z et al. TRiC/CCT Chaperonin Governs RNA Polymerase II Activity in the Nucleus… bioRxiv preprint. Sep 26, 2024. https://doi.org/10.1101/2024.09.26.615188 (gvozdenov2024triccctchaperoningoverns pages 1-6)

References

1. (grantham2020themolecularchaperone pages 1-2): Julie Grantham. The molecular chaperone cct/tric: an essential component of proteostasis and a potential modulator of protein aggregation. Frontiers in Genetics, Mar 2020. URL: https://doi.org/10.3389/fgene.2020.00172, doi:10.3389/fgene.2020.00172. This article has 139 citations and is from a peer-reviewed journal.

2. (dube2023saccharomycescerevisiaesurvival pages 1-4): Ankita Dube, Dileep Pullepu, and M. Anaul Kabir. Saccharomyces cerevisiae survival against heat stress entails a communication between cct and cell wall integrity pathway. Biologia futura, 74:519-527, Nov 2023. URL: https://doi.org/10.1007/s42977-023-00192-1, doi:10.1007/s42977-023-00192-1. This article has 2 citations and is from a peer-reviewed journal.

3. (kabir2005physiologicaleffectsof pages 1-2): M. Anaul Kabir, Joanna Kaminska, George B. Segel, Gabor Bethlendy, Paul Lin, Flavio Della Seta, Casey Blegen, Kristine M. Swiderek, Teresa ?o??dek, Kim T. Arndt, and Fred Sherman. Physiological effects of unassembled chaperonin cct subunits in the yeast saccharomyces cerevisiae. Yeast, 22:219-239, Feb 2005. URL: https://doi.org/10.1002/yea.1210, doi:10.1002/yea.1210. This article has 60 citations and is from a peer-reviewed journal.

4. (kabir2005physiologicaleffectsof pages 2-4): M. Anaul Kabir, Joanna Kaminska, George B. Segel, Gabor Bethlendy, Paul Lin, Flavio Della Seta, Casey Blegen, Kristine M. Swiderek, Teresa ?o??dek, Kim T. Arndt, and Fred Sherman. Physiological effects of unassembled chaperonin cct subunits in the yeast saccharomyces cerevisiae. Yeast, 22:219-239, Feb 2005. URL: https://doi.org/10.1002/yea.1210, doi:10.1002/yea.1210. This article has 60 citations and is from a peer-reviewed journal.

5. (zang2018developmentofa pages 1-2): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.

6. (kabir2008overexpressedribosomalproteins pages 1-2): M. Anaul Kabir and Fred Sherman. Overexpressed ribosomal proteins suppress defective chaperonins in saccharomyces cerevisiae. FEMS yeast research, 8 8:1236-44, Dec 2008. URL: https://doi.org/10.1111/j.1567-1364.2008.00425.x, doi:10.1111/j.1567-1364.2008.00425.x. This article has 21 citations and is from a peer-reviewed journal.

7. (kelly2020structuralandfunctional pages 18-23): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

8. (willison2018thestructureand pages 1-2): Keith Robert Willison. The structure and evolution of eukaryotic chaperonin-containing tcp-1 and its mechanism that folds actin into a protein spring. The Biochemical journal, 475 19:3009-3034, Oct 2018. URL: https://doi.org/10.1042/bcj20170378, doi:10.1042/bcj20170378. This article has 42 citations.

9. (kelly2020structuralandfunctionala pages 42-48): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

10. (kelly2020structuralandfunctional pages 42-48): J Kelly. Structural and functional characterisation of the group ii chaperonin cct/tric. Unknown journal, 2020.

11. (dube2021chaperoninpointmutation pages 1-4): Ankita Dube and M. Anaul Kabir. Chaperonin point mutation enhances cadmium endurance in saccharomyces cerevisiae. Biotechnology Letters, 43:1735-1745, May 2021. URL: https://doi.org/10.1007/s10529-021-03151-9, doi:10.1007/s10529-021-03151-9. This article has 2 citations and is from a peer-reviewed journal.

12. (zang2018developmentofa media 20a150a9): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.

13. (kabir2008overexpressedribosomalproteins pages 2-3): M. Anaul Kabir and Fred Sherman. Overexpressed ribosomal proteins suppress defective chaperonins in saccharomyces cerevisiae. FEMS yeast research, 8 8:1236-44, Dec 2008. URL: https://doi.org/10.1111/j.1567-1364.2008.00425.x, doi:10.1111/j.1567-1364.2008.00425.x. This article has 21 citations and is from a peer-reviewed journal.

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16. (roy2023reducedadpoffrate pages 1-2): Mousam Roy, Rachel C. Fleisher, Alexander I. Alexandrov, and Amnon Horovitz. Reduced adp off-rate by the yeast cct2 double mutation t394p/r510h which causes leber congenital amaurosis in humans. Communications Biology, Aug 2023. URL: https://doi.org/10.1038/s42003-023-05261-8, doi:10.1038/s42003-023-05261-8. This article has 9 citations and is from a peer-reviewed journal.

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