• Drosophila melanogaster chaperonin containing TCP1 subunit 5, transcript variant A (CCT5), mRNA. (genscript.com)
  • The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). (nih.gov)
  • chaperonin-containing T-complex epsilon subunit Cct5. (ntu.edu.sg)
  • The chaperonin family includes the mitochondrial HSP60, Escherichia coli GroEL, the plastid Rubisco-subunit binding protein, and the archaebacterial protein TF55. (thermofisher.cn)
  • The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins. (yeastgenome.org)
  • In the present study, we show that the eukaryotic cytosolic chaperonin CCT [chaperonin containing TCP-1 (tailless complex polypeptide 1)] binds to newly synthesized eIF3b and promotes the correct folding of eIF3h and eIF3i. (manchester.ac.uk)
  • Recent structural data suggest an effective size limit for the TRiC folding chamber of ∼70 kDa, but numerous chaperonin substrates are substantially larger. (cipsm.de)
  • Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). (nih.gov)
  • Hsp60 household The Hsp60 relatives is definitely the most studied of each of the chaperone families and is composed of GroEL and its homologues in prokaryotes, chloroplasts and mitochondria, along with the TRiC TCP 1 family members while in the eukaryotic cytosol. (screeninglibraries.com)
  • Cytoskeleton.actin and tubulin folding.CCT chaperonin. (ntu.edu.sg)
  • The eukaryotic chaperonin-containing TCP-1 (CCT) folds the cytoskeletal protein actin. (icr.ac.uk)
  • The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo. (google.ro)
  • In the present report, we show that, after exposure to nicotine for 14 days, ubiquitin, ubiquitin-conjugating enzymes, 20S and 19S proteasomal subunits, and chaperonin-containing TCP-1 protein (CCT) complex members are upregulated in rat prefrontal cortex (PFC) while being downregulated in the medial basal hypothalamus (MBH). (bilkent.edu.tr)
  • The family of proteins termed chaperonins act to recognize and stabilize polypeptide intermediates during folding, assembly and disassembly, and share many characteristics with Heat Shock Protein 70 (HSP70) including high abundance, induction by environmental stress, and ATPase activity. (thermofisher.cn)
  • The results showed that chaperonin containing tailless complex polypeptide the large number of proteins involved, the complex relationship between proteins and the lack of research on the effects of movement and cell protein folding and degradation. (ijpsonline.com)
  • Chaperonin Containing Tailless Complex Polypeptide 1 (CCT-1) is one of the important elements of protein folding pathway in cells and proteasome is an important component of Adenosine Triphosphate (ATP) dependent protein degradation pathway in cells. (ijpsonline.com)
  • The T Complex Polypeptide 1 (TCP-1) is approximately 60 kDa protein constitutively expressed in almost all eukaryotic cells, and is upregulated during spermatogenesis. (thermofisher.cn)
  • The TCP-1 sequence shows nearly 40% identity to TF55, but only minimal similarity to HSP60 and GroEL. (thermofisher.cn)
  • In this brief review, we describe some paradigmatic examples pertaining to the chaperonins Hsp60 (HSPD1, or HSP60, or Cpn60) and CCT (chaperonin-containing TCP-1). (unipa.it)
  • [ 10 ] In this study, molecular characterization of thermotolerant or thermophilic members of the family Trichocomaceae including G. argillacea , Talaromyces emersonii and Talaromyces byssochlamydoides was conducted using partial RPB2 (RNA polymerase II gene), Tsr1 (putative ribosome biogenesis protein) and Cct8 (putative chaperonin complex component TCP-1) gene sequences, and the results were combined with observations of morphological and physiological features. (medscape.com)
  • The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). (nih.gov)
  • We have previously demonstrated the ability of I-Trp to disrupt the protein-protein interaction of β-tubulin with chaperonin-containing TCP-1β (CCT-β). (tmu.edu.tw)
  • The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. (bvsalud.org)
  • She performs integrative Protein folding and Chaperonin research in her work. (research.com)
  • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. (research.com)
  • Chaperonin formulated with T-complex proteins-1 (CCT) is among the eukaryotic chaperon systems categorized into group II chaperonin.6 Eight genes (mutations, mutations in other genes encoding CCT subunits have already been identified in human beings, animals, and fungus. (rawveronica.com)
  • Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). (nih.gov)
  • Melkani and Gill repeated their experiments using mutant strains of flies with nonfunctional versions of the TCP-1 and circadian rhythm genes. (sciencedaily.com)
  • Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies. (nih.gov)
  • CCT8L2 belongs to the TCP-1 chaperonin family. (clonagen.com)