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protein_family: Belongs to the TCP-1 chaperonin family. .
protein_domains: Chap_CCT_beta. (IPR012716); 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: P39076
• Protein Description: RecName: Full=T-complex protein 1 subunit beta; Short=TCP-1-beta; AltName: Full=CCT-beta;
• Gene Information: Name=CCT2; Synonyms=BIN3, TCP2; OrderedLocusNames=YIL142W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_beta. (IPR012716); 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 "CCT2" 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 'CCT2' 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 CCT2 (gene ID: CCT2, UniProt: P39076) 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: P39076
• Protein Description: RecName: Full=T-complex protein 1 subunit beta; Short=TCP-1-beta; AltName: Full=CCT-beta;
• Gene Information: Name=CCT2; Synonyms=BIN3, TCP2; OrderedLocusNames=YIL142W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_beta. (IPR012716); 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 "CCT2" 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 'CCT2' 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 CCT2 (gene ID: CCT2, UniProt: P39076) 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.

Comprehensive Research Report: Saccharomyces cerevisiae CCT2 (UniProt P39076; ORF YIL142W) — Functional Annotation

1. Gene/Protein Identity Verification (mandatory disambiguation)

Target identity confirmed: In Saccharomyces cerevisiae (S288c), CCT2 corresponds to ORF YIL142W and encodes the T-complex protein 1 subunit beta (also referred to as TCP-1-beta / CCT-beta), a core subunit of the cytosolic chaperonin CCT/TRiC. Synonyms reported in yeast literature include BIN3 and TCP1b/Cctb. This mapping and nomenclature are explicitly documented in the yeast CCT subunit review that lists CCT2 as YIL142W and identifies it as the beta-type TCP-1/CCT subunit. (stoldt1996reviewthecct pages 1-2, stoldt1996reviewthecct pages 2-4)

2. Key Concepts and Definitions (current understanding)

2.1 What is CCT/TRiC?

CCT/TRiC (Chaperonin Containing TCP-1; TCP-1 Ring Complex) is the eukaryotic Group II cytosolic chaperonin. It forms an ATP-dependent protein-folding machine built as a double-ring complex (two stacked rings) with eight distinct subunits per ring (Cct1p–Cct8p), arranged in a fixed order. (kabir2005physiologicaleffectsof pages 1-2, willison2018thesubstratespecificity pages 1-2)

2.2 Where does Cct2p fit into the complex?

Cct2p (CCT2) is one of the eight essential subunits that assemble into the full CCT/TRiC complex. Each subunit has a conserved chaperonin fold with three domains:
- Equatorial domain (contains the ATP-binding site)
- Intermediate domain
- Apical domain (major substrate-binding determinants)
Subunit-to-subunit sequence variation is concentrated in the apical domains, supporting subunit-specific substrate recognition. (willison2018thesubstratespecificity pages 1-2, willison2018thestructureand pages 4-6, kabir2005physiologicaleffectsof pages 1-2)

2.3 Mechanistic overview (ATPase cycle, substrate recognition)

CCT/TRiC operates through an ATP-driven conformational cycle that couples ATP binding/hydrolysis to lid closure and substrate encapsulation in the central cavity (a built-in lid is a Group II hallmark). The cycle is asymmetric/sequential across the eight subunits rather than uniform, consistent with subunit-specific ATP affinities and coordinated allostery. (ghozlan2022thetrickybusiness pages 5-6, kabir2005physiologicaleffectsof pages 1-2, willison2018thesubstratespecificity pages 1-2)

A mechanistic detail relevant to Cct2: actin binding is described as preferentially involving the CCT2 side of the complex, and sequential ATP binding/hydrolysis is inferred to initiate on that side in some models, consistent with asymmetric folding pathways. (ghozlan2022thetrickybusiness pages 5-6)

3. Primary Function of CCT2 in Yeast (substrates and biological role)

3.1 Core biochemical function: ATP-dependent folding of obligate cytosolic clients

The primary function of yeast Cct2p is as a structural and catalytic component of the CCT/TRiC chaperonin that produces folding-competent forms of essential cytosolic proteins.

Best-supported client classes include:
- Actin and tubulin, which are repeatedly emphasized as major/obligate substrates of TRiC/CCT across eukaryotes, and yeast conditional mutants show cytoskeletal phenotypes consistent with defects in actin and microtubule assembly. (stoldt1996reviewthecct pages 2-4, willison2018thesubstratespecificity pages 1-2)

3.2 Cytoskeletal organization phenotypes in cct2 mutants

Conditional alleles cct2-1 through cct2-4 cause growth arrest at restrictive conditions with cytoskeletal disorganization, including disruptions of microtubule-mediated processes and altered actin/microtubule assemblies in the mutant series. These phenotypes support that proper Cct2p function is required for cytoskeletal proteostasis in vivo. (stoldt1996reviewthecct pages 2-4)

A distinct engineered ATPase-site perturbation of CCT2 (Asp→Glu substitution introduced analogously across subunits) produced heat and cold sensitivity, excess actin patches, and a pseudo-diploid state, highlighting a strong coupling between Cct2p ATPase function and actin organization/cell physiology. (amit2010equivalentmutationsin pages 1-2)

3.3 ATP-binding motif integrity is critical (cct2-3)

A specific allele cct2-3 alters the conserved ATP-binding motif GDGTT and is described as producing strong phenotypes. Genetic suppression of cct2-3 by a mutation in another subunit (cct6-3, L19S) indicates functional coupling among subunits and suggests that assembly/cycle defects can sometimes be compensated by altered subunit interactions. (kabir2005physiologicaleffectsof pages 1-2)

4. Cellular Localization and Pathway Context

4.1 Canonical localization: cytosolic proteostasis hub

CCT/TRiC is classically considered a cytosolic chaperonin central to folding/assembly of cytoskeletal and other complex substrates. Its broad genetic/physical interaction network connects it to diverse pathways (cytoskeleton, cell cycle regulators, and other essential complexes). (willison2018thesubstratespecificity pages 1-2, willison2018thesubstratespecificity pages 6-7)

4.2 Recent yeast nuclear localization and nuclear pathway role (2024)

A major 2024 development is evidence that assembled TRiC/CCT is present in the yeast nucleus, shown using Cct2-GFP and Cct6-GFP fusions with microscopy, biochemical fractionation, and size-exclusion chromatography consistent with a ~1 MDa holo-complex in nuclear fractions. (gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 21-25)

In the same 2024 preprint, TRiC/CCT is proposed to act as a rheostat for RNA polymerase II activity, supporting RNA homeostasis by limiting cryptic/noncoding transcription. Functional perturbation (temperature-sensitive cct1-2 at 37°C for 4 h) caused widespread noncoding RNA accumulation with modest ORF-level changes. Nuclear depletion experiments (GAL1-driven NES nanobody exporting Cct2/Cct6-GFP) further support a nucleus-specific role. (gvozdenov2024triccctchaperoningoverns pages 21-25, gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 25-30)

Interpretation: Although the perturbation allele is cct1-2, the experiments rely directly on Cct2-GFP to establish nuclear localization and nuclear depletion strategies, making this a relevant and recent yeast context for CCT2’s cellular geography and pathway reach. (gvozdenov2024triccctchaperoningoverns pages 21-25, gvozdenov2024triccctchaperoningoverns pages 6-9)

5. Interaction Partners and Network Position (yeast experimental evidence)

5.1 Affinity purification/mass spectrometry identifies Cct2p in assembled CCT complexes

In large-scale yeast CCT interaction mapping, Cct2p is robustly detected in purified CCT complexes (MudPIT scores reported for CCT2 in both ATP-dependent and non-ATP conditions). The same purifications identify known substrates/partners, including actin, β-tubulin, and (notably) a set of septin GTPases, supporting that CCT engages cytoskeletal systems beyond actin/tubulin. (dekker2008theinteractionnetwork pages 2-3, dekker2008theinteractionnetwork pages 3-4)

CCT2 is also among subunits specifically scored in these preparations, providing direct physical evidence that the protein is part of the purified yeast CCT machine. (dekker2008theinteractionnetwork pages 2-3, dekker2008theinteractionnetwork pages 3-4)

5.2 Genetic coupling to actin and other essential functions

A quantitative genetic synthesis summarized in a major review reports that CCT2 is strongly positively epistatic with ACT1 and also with NUS1, RPC10, and RP55, supporting a tight functional relationship between the CCT2-containing chaperonin and actin-dependent biology and potentially additional essential processes. (willison2018thesubstratespecificity pages 6-7)

6. Recent Developments (prioritizing 2023–2024)

6.1 2024: Nuclear TRiC/CCT control of RNAP II and RNA homeostasis

The 2024 bioRxiv study provides multiple lines of evidence (RNA-Seq, 4tU-Seq, DNaseI-Seq, histone PTM mass spectrometry, ChIP, in vitro transcription) that TRiC/CCT affects transcription output and RNA stability/termination.

Key reported quantitative outcomes include:
- Genome-associated noncoding RNAs increased from ~0.3% (parental) to ~9.8% in cct1-2, and intergenic coverage increased from ~4% to ~65%. (gvozdenov2024triccctchaperoningoverns pages 6-9)
- Nearly half of snoRNA loci showed readthrough: 30/68 snoRNA genes with ~1.5× increased readthrough. (gvozdenov2024triccctchaperoningoverns pages 9-13, gvozdenov2024triccctchaperoningoverns pages 6-9)
- Nascent transcription increased strongly: ~22.8% of the genome had ≥4-fold higher nascent RNA signal. (gvozdenov2024triccctchaperoningoverns pages 13-17)
- In vitro transcription from nuclear extracts: cct1-2 extract produced ~10× more RNA, and adding purified recombinant TRiC in the 5–100 nM range restored RNAP II activity toward WT. (gvozdenov2024triccctchaperoningoverns pages 21-25, gvozdenov2024triccctchaperoningoverns pages 13-17)

These findings extend yeast TRiC/CCT biology beyond canonical cytosolic folding into nuclear gene-expression regulation, with Cct2 as an experimentally tracked subunit (GFP fusions; nuclear depletion strategy). (gvozdenov2024triccctchaperoningoverns pages 21-25, gvozdenov2024triccctchaperoningoverns pages 6-9)

6.2 2023: Stress-pathway coupling between TRiC/CCT and cell wall integrity (CWI) MAPK signaling

A 2023 yeast study shows that a TRiC/CCT folding defect (cct7 G412E) causes temperature sensitivity and cell wall stress sensitivity, and that overexpression of CWI pathway kinases PKC1 or SLT2 rescues growth defects, indicating functional coupling between proteostasis capacity and cell wall integrity signaling in yeast stress tolerance. (dube2023saccharomycescerevisiaesurvival pages 4-7, dube2023saccharomycescerevisiaesurvival pages 1-4)

7. Current Applications and Real-World Implementations (yeast-relevant)

Direct industrial “implementations” specifically targeting CCT2 are not well represented in the retrieved corpus; however, multiple yeast studies provide actionable engineering principles involving the CCT/TRiC system that are directly relevant to biotechnology contexts (fermentation robustness; stress tolerance; proteostasis management).

7.1 Ethanol tolerance and cell wall robustness

Defects in TRiC/CCT protein folding machinery (including strains using CCT1/CCT2 alleles) are associated with cell wall defects and reduced tolerance to ethanol, connecting chaperonin function to traits central to industrial yeast performance (stress resistance, membrane/cell wall integrity). Extragenic suppressors that improve growth on ethanol in a severe CCT allele background were identified (RPS6A, SCL1, TDH3 overexpression), suggesting routes to compensate folding defects. (narayanan2016defectsinprotein pages 1-2)

7.2 Heat stress and CWI pathway rescue as an engineering handle

In the cct7 G412E background (a TRiC folding defect model), CWI pathway activation provides a tunable rescue. Quantitatively, PKC1 overexpression reduced doubling time from 8.4 h to 3.9 h, and SLT2 overexpression reduced doubling time to 5.5 h (wild type 3.2 h), illustrating that stress-performance deficits arising from impaired chaperonin activity can be partially restored by pathway engineering. (dube2023saccharomycescerevisiaesurvival pages 4-7)

7.3 Heavy-metal tolerance phenotypes as a systems-level outcome of chaperonin perturbation

A TRiC perturbation in yeast (Cct7 ATP-binding pocket mutation) produced increased cadmium uptake (10.59 µg Cd per mg) and induced vacuolar transporters (~10× YCF1 and ~2× BPT1), highlighting that proteostasis perturbations can rewire stress responses and metal handling—potentially relevant for bioremediation or stress-resilient strain design, though with noted trade-offs (e.g., lethality under arsenite). (dube2021chaperoninpointmutation pages 1-4)

8. Expert Opinions and Authoritative Interpretations

Multiple authoritative reviews emphasize that CCT/TRiC is a selective but central proteostasis hub with strong genetic sensitivity to subunit dosage and critical control over actin/tubulin folding flux.

• Willison (2018) frames yeast CCT as abundant but limiting relative to ribosomes and argues that actin/tubulin occupy a dominant share of CCT folding capacity, implying that modest perturbations can have system-wide consequences for cytoskeletal and cell-cycle function. (willison2018thesubstratespecificity pages 6-7)
• Reviews also emphasize CCT/TRiC’s subunit asymmetry and sequential allostery, consistent with the observation that subunit-specific ATPase perturbations (including in CCT2) yield dramatically different phenotypes rather than uniform loss-of-function effects. (ghozlan2022thetrickybusiness pages 5-6, amit2010equivalentmutationsin pages 1-2)

9. Key Statistics and Data (recent and foundational)

Selected quantitative facts relevant to yeast CCT2 functional annotation:

• Cellular abundance: ~3,000–6,000 CCT complexes per yeast cell. (willison2018thesubstratespecificity pages 6-7)
• Functional occupancy: ~50–60% of CCT engaged with actin/tubulin folding. (willison2018thesubstratespecificity pages 6-7)
• Expression estimate: CCT2 mRNA ~1.56 copies/cell (dataset summarized in review). (willison2018thesubstratespecificity pages 7-8)
• Interaction network scale: CCT interactome estimated ~300 genes/proteins in yeast synthesis; AP-MS interaction network reported 136 interacting proteins/genes and 227 interactions in an expanded dataset. (willison2018thesubstratespecificity pages 6-7, dekker2008theinteractionnetwork pages 8-9)
• AP-MS identification: CCT2 MudPIT score ~4409 (no ATP dataset) and 4560 (ATP-elutable dataset), measured mass ~57,510 Da. (dekker2008theinteractionnetwork pages 2-3, dekker2008theinteractionnetwork pages 3-4)
• Nuclear TRiC perturbation consequences (2024 preprint): noncoding RNA genome association ~0.3% → 9.8%; intergenic coverage ~4% → 65%; 30/68 snoRNAs with ~1.5× readthrough; 22.8% genome with ≥4× nascent RNAs; in vitro transcription ~10× higher; rescue with 5–100 nM recombinant TRiC. (gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 9-13, gvozdenov2024triccctchaperoningoverns pages 13-17, gvozdenov2024triccctchaperoningoverns pages 21-25)

10. Evidence Map (summary table)

Table: This table summarizes the main functional annotation evidence for yeast CCT2/YIL142W, from gene identity and essentiality to folding function, mutant phenotypes, interaction networks, and recent nuclear/RNA homeostasis findings. It is useful as a compact evidence map linking each annotation claim to specific literature and context IDs.

11. Conclusion (functional annotation statement)

CCT2 (Cct2p; UniProt P39076; YIL142W) is an essential subunit of the yeast cytosolic Group II chaperonin CCT/TRiC, whose primary role is to support ATP-dependent folding/biogenesis of key cytoskeletal proteins (especially actin and tubulin) and thereby maintain cytoskeletal organization and viability. Yeast genetic evidence (conditional cct2 allele series; ATP-binding motif mutant cct2-3; engineered ATPase-site substitution) demonstrates that perturbing Cct2p produces strong growth and cytoskeletal phenotypes consistent with impaired CCT function. Physical interaction studies confirm Cct2p’s presence in purified CCT complexes associated with known clients/partners (actin, tubulin, septins). Recent 2024 yeast work expands the functional landscape by placing assembled TRiC/CCT (tracked using Cct2-GFP) in the nucleus, where it can modulate RNA polymerase II output and RNA homeostasis, suggesting that CCT2-containing TRiC complexes contribute to both cytosolic proteostasis and nuclear gene-expression control. (stoldt1996reviewthecct pages 2-4, kabir2005physiologicaleffectsof pages 1-2, amit2010equivalentmutationsin pages 1-2, dekker2008theinteractionnetwork pages 3-4, willison2018thesubstratespecificity pages 6-7, gvozdenov2024triccctchaperoningoverns pages 6-9, gvozdenov2024triccctchaperoningoverns pages 21-25)

References (URLs and publication dates)

• Stoldt V. et al. May 1996. Yeast. “Review: The Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts.” https://doi.org/10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c (stoldt1996reviewthecct pages 1-2, stoldt1996reviewthecct pages 2-4)
• Kabir M.A. et al. Feb 2005. Yeast. “Physiological effects of unassembled chaperonin Cct subunits…” https://doi.org/10.1002/yea.1210 (kabir2005physiologicaleffectsof pages 1-2)
• Dekker C. et al. Jul 2008. EMBO Journal. “The interaction network of the chaperonin CCT.” https://doi.org/10.1038/emboj.2008.108 (dekker2008theinteractionnetwork pages 2-3, dekker2008theinteractionnetwork pages 8-9, dekker2008theinteractionnetwork pages 3-4)
• Amit M. et al. Aug 2010. Journal of Molecular Biology. “Equivalent mutations in the eight subunits…” https://doi.org/10.1016/j.jmb.2010.06.037 (amit2010equivalentmutationsin pages 1-2)
• Willison K.R. Jun 2018. Philosophical Transactions of the Royal Society B. “The substrate specificity of eukaryotic cytosolic chaperonin CCT.” https://doi.org/10.1098/rstb.2017.0192 (willison2018thesubstratespecificity pages 1-2, willison2018thesubstratespecificity pages 6-7, willison2018thesubstratespecificity pages 7-8)
• Ghozlan H. et al. May 2022. Frontiers in Cell and Developmental Biology. “The TRiCky Business of Protein Folding in Health and Disease.” https://doi.org/10.3389/fcell.2022.906530 (ghozlan2022thetrickybusiness pages 5-6, ghozlan2022thetrickybusiness pages 1-2)
• Dube A. et al. Nov 2023. Biologia Futura. “Survival against heat stress entails a communication between CCT and cell wall integrity pathway.” https://doi.org/10.1007/s42977-023-00192-1 (dube2023saccharomycescerevisiaesurvival pages 4-7, dube2023saccharomycescerevisiaesurvival pages 1-4)
• Que Y. et al. Apr 2024. Heliyon. “The role of molecular chaperone CCT/TRiC in translation elongation: A literature review.” https://doi.org/10.1016/j.heliyon.2024.e29029 (que2024theroleof pages 7-9)
• Gvozdenov Z. et al. Sep 26, 2024. bioRxiv (preprint). “TRiC/CCT Chaperonin Governs RNA Polymerase II Activity…” https://doi.org/10.1101/2024.09.26.615188 (gvozdenov2024triccctchaperoningoverns pages 25-30, gvozdenov2024triccctchaperoningoverns pages 21-25, gvozdenov2024triccctchaperoningoverns pages 9-13, gvozdenov2024triccctchaperoningoverns pages 13-17, gvozdenov2024triccctchaperoningoverns pages 6-9)
• Narayanan A. et al. Mar 2016. Current Microbiology. “Defects in protein folding machinery affect cell wall integrity and reduce ethanol tolerance…” https://doi.org/10.1007/s00284-016-1024-x (narayanan2016defectsinprotein pages 1-2)
• Dube A., Kabir M.A. May 2021. Biotechnology Letters. “Chaperonin point mutation enhances cadmium endurance…” https://doi.org/10.1007/s10529-021-03151-9 (dube2021chaperoninpointmutation pages 1-4)

References

1. (stoldt1996reviewthecct pages 1-2): Volker Stoldt, Felicitas Rademacher, Verena Kehren, Joachim F. Ernst, David A. Pearce, and Fred Sherman. Review: the cct eukaryotic chaperonin subunits of saccharomyces cerevisiae and other yeasts. Yeast, 12:523-529, May 1996. URL: https://doi.org/10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c, doi:10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c. This article has 153 citations and is from a peer-reviewed journal.

2. (stoldt1996reviewthecct pages 2-4): Volker Stoldt, Felicitas Rademacher, Verena Kehren, Joachim F. Ernst, David A. Pearce, and Fred Sherman. Review: the cct eukaryotic chaperonin subunits of saccharomyces cerevisiae and other yeasts. Yeast, 12:523-529, May 1996. URL: https://doi.org/10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c, doi:10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c. This article has 153 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. (willison2018thesubstratespecificity pages 1-2): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

5. (willison2018thestructureand pages 4-6): 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.

6. (ghozlan2022thetrickybusiness pages 5-6): Heba Ghozlan, Amanda Cox, Daniel Nierenberg, Stephen King, and Annette R. Khaled. The tricky business of protein folding in health and disease. Frontiers in Cell and Developmental Biology, May 2022. URL: https://doi.org/10.3389/fcell.2022.906530, doi:10.3389/fcell.2022.906530. This article has 34 citations.

7. (amit2010equivalentmutationsin pages 1-2): Maya Amit, Sarah J. Weisberg, Michal Nadler-Holly, Elizabeth A. McCormack, Ester Feldmesser, Daniel Kaganovich, Keith R. Willison, and Amnon Horovitz. Equivalent mutations in the eight subunits of the chaperonin cct produce dramatically different cellular and gene expression phenotypes. Journal of molecular biology, 401 3:532-43, Aug 2010. URL: https://doi.org/10.1016/j.jmb.2010.06.037, doi:10.1016/j.jmb.2010.06.037. This article has 117 citations and is from a domain leading peer-reviewed journal.

8. (willison2018thesubstratespecificity pages 6-7): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

9. (gvozdenov2024triccctchaperoningoverns pages 6-9): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

10. (gvozdenov2024triccctchaperoningoverns pages 21-25): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

11. (gvozdenov2024triccctchaperoningoverns pages 25-30): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

12. (dekker2008theinteractionnetwork pages 2-3): Carien Dekker, Peter C Stirling, Elizabeth A McCormack, Heather Filmore, Angela Paul, Renee L Brost, Michael Costanzo, Charles Boone, Michel R Leroux, and Keith R Willison. The interaction network of the chaperonin cct. The EMBO Journal, 27:1827-1839, Jul 2008. URL: https://doi.org/10.1038/emboj.2008.108, doi:10.1038/emboj.2008.108. This article has 255 citations.

13. (dekker2008theinteractionnetwork pages 3-4): Carien Dekker, Peter C Stirling, Elizabeth A McCormack, Heather Filmore, Angela Paul, Renee L Brost, Michael Costanzo, Charles Boone, Michel R Leroux, and Keith R Willison. The interaction network of the chaperonin cct. The EMBO Journal, 27:1827-1839, Jul 2008. URL: https://doi.org/10.1038/emboj.2008.108, doi:10.1038/emboj.2008.108. This article has 255 citations.

14. (gvozdenov2024triccctchaperoningoverns pages 9-13): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

15. (gvozdenov2024triccctchaperoningoverns pages 13-17): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

16. (dube2023saccharomycescerevisiaesurvival pages 4-7): 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.

17. (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.

18. (narayanan2016defectsinprotein pages 1-2): Aswathy Narayanan, Dileep Pullepu, Praveen Kumar Reddy, Wasim Uddin, and M. Anaul Kabir. Defects in protein folding machinery affect cell wall integrity and reduce ethanol tolerance in s. cerevisiae. Current Microbiology, 73:38-45, Mar 2016. URL: https://doi.org/10.1007/s00284-016-1024-x, doi:10.1007/s00284-016-1024-x. This article has 7 citations and is from a peer-reviewed journal.

19. (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.

20. (willison2018thesubstratespecificity pages 7-8): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

21. (dekker2008theinteractionnetwork pages 8-9): Carien Dekker, Peter C Stirling, Elizabeth A McCormack, Heather Filmore, Angela Paul, Renee L Brost, Michael Costanzo, Charles Boone, Michel R Leroux, and Keith R Willison. The interaction network of the chaperonin cct. The EMBO Journal, 27:1827-1839, Jul 2008. URL: https://doi.org/10.1038/emboj.2008.108, doi:10.1038/emboj.2008.108. This article has 255 citations.

22. (willison2018thesubstratespecificity pages 6-6): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

23. (dekker2008theinteractionnetwork pages 5-6): Carien Dekker, Peter C Stirling, Elizabeth A McCormack, Heather Filmore, Angela Paul, Renee L Brost, Michael Costanzo, Charles Boone, Michel R Leroux, and Keith R Willison. The interaction network of the chaperonin cct. The EMBO Journal, 27:1827-1839, Jul 2008. URL: https://doi.org/10.1038/emboj.2008.108, doi:10.1038/emboj.2008.108. This article has 255 citations.

24. (ghozlan2022thetrickybusiness pages 1-2): Heba Ghozlan, Amanda Cox, Daniel Nierenberg, Stephen King, and Annette R. Khaled. The tricky business of protein folding in health and disease. Frontiers in Cell and Developmental Biology, May 2022. URL: https://doi.org/10.3389/fcell.2022.906530, doi:10.3389/fcell.2022.906530. This article has 34 citations.

25. (que2024theroleof pages 7-9): Yueyue Que, Yudan Qiu, Zheyu Ding, Shanshan Zhang, Rong Wei, Jianing Xia, and Yingying Lin. The role of molecular chaperone cct/tric in translation elongation: a literature review. Heliyon, 10:e29029, Apr 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e29029, doi:10.1016/j.heliyon.2024.e29029. This article has 12 citations.

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