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TRiC (complex)
T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates. TRiC is an example of a biological machine that folds substrates within the central cavity of its barrel-like assembly using the energy from ATP hydrolysis. Subunits The human TRiC complex is formed by two rings containing 8 similar but non-identical subunits, each with molecular weights of ~60 kDa. The two rings are stacked in an asymmetrical fashion, forming a barrel-like structure with a molecular weight of ~1 MDa. Molecular weight of human subunits. Counterclockwise from the exterior, each ring is made of the subunits in the following order: 6-8-7-5-2-4-1-3. Evolution The CCT evolved from the archaeal thermosome ~2Gya, with the two subunits diversifying into multi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCT5 (gene)
T-complex protein 1 subunit epsilon is a protein that in humans is encoded by the ''CCT5'' gene. Function This gene encodes a molecular chaperone that is member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. Interactions CCT5 (gene) has been shown to interact with PPP4C Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the ''PPP4C'' gene. Interactions PPP4C has been shown to interact with: * CCDC6, * CCT2, * CCT3, * CCT4, * CCT5, * CCT6A, * CCT7, * IG .... References External links * Further reading * * * * * * * * * * * * * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Molecular Biology
Molecular biology is the branch of biology that seeks to understand the molecular basis of biological activity in and between cells, including biomolecular synthesis, modification, mechanisms, and interactions. The study of chemical and physical structure of biological macromolecules is known as molecular biology. Molecular biology was first described as an approach focused on the underpinnings of biological phenomena - uncovering the structures of biological molecules as well as their interactions, and how these interactions explain observations of classical biology. In 1945 the term molecular biology was used by physicist William Astbury. In 1953 Francis Crick, James Watson, Rosalind Franklin, and colleagues, working at Medical Research Council unit, Cavendish laboratory, Cambridge (now the MRC Laboratory of Molecular Biology), made a double helix model of DNA which changed the entire research scenario. They proposed the DNA structure based on previous research done by Ro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heat Shock Protein
Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). HSPs are found in virtually all living organisms, from bacteria to humans. Heat-shock proteins are named according to their molecular weight. For example, HSP60, Hsp60, Hsp70 and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70 and 90 ato ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chaperonin
HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called molecular chaperones. Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional tertiary structure. The energy to fold proteins is supplied by non-covalent interactions between the amino acid side chains of each protein, and by solvent effects. Most proteins spontaneously fold into their most stable three-dimensional conformation, which is usually also their functional conformation, but occasionally proteins mis-fold. Molecular chaperones catalyze protein refolding by accelerating partial unfolding of misfolded proteins, aided by energy supplied by the hydrolysis of adenosine triphosphate (ATP). Chaperonin proteins may also tag ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chaperone (protein)
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress. The majority of molecular chaperones do not convey any steric information for protein folding, and instead assist in protein folding by binding to and stabilizing folding interme ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thermosome
A thermosome is a group II chaperonin protein complex that functions in archaea. It is the homolog of eukaryotic CCT. This group II chaperonin is an ATP-dependent chaperonin that is responsible for folding or refolding of incipient or denatured proteins. A thermosome has two rings, each consisting of eight subunits, stacked together to form a cylindrical shape with a large cavity at the center. The thermosome is also defined by its heterooligomeric nature. The complex consists of that alternate location within its two rings. Being a Group II chaperonin, the thermosome has a similar structure to group I chaperonins. The main difference, however, lies in the existence of a helical protrusion in the thermosome which composes of a built-in lid of the hydrophilic cavity. Not only is thermosome ATP-dependent, but the mechanism in which thermosome shifts from open to close conformation is also temperature-dependent. The open conformation of the ATP-thermosome exists mainly at ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCT8
T-complex protein 1 subunit theta is a protein that in humans is encoded by the ''CCT8'' gene. The CCT8 protein is a component of the TRiC complex. See also * TCP1, T-complex protein 1 subunit alpha * Chaperonin HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 bel ... References External links * Further reading * * * * * * * * * * * * * * * * * {{gene-21-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCT7
T-complex protein 1 subunit eta is a protein that in humans is encoded by the ''CCT7'' gene. Function This gene encodes a molecular chaperone that is a member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants encoding different isoforms have been found for this gene, but only two of them have been characterized to date. Interactions CCT7 has been shown to interact with PPP4C Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the ''PPP4C'' gene. Interactions PPP4C has been shown to interact with: * CCDC6, * CCT2, * CCT3, * CCT4, * CCT5, * CCT6A, * CCT7, * IG .... References External links * Further reading * * * * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCT6B
T-complex protein 1 subunit zeta-2 is a protein that in humans is encoded by the ''CCT6B'' gene. This gene encodes a molecular chaperone that is a member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoske .... Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. References External links * Further reading * * * * * * {{gene-17-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCT6A
T-complex protein 1 subunit zeta is a protein that in humans is encoded by the ''CCT6A'' gene. Function This gene encodes a molecular chaperone that is member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. Interactions CCT6A has been shown to interact with PPP4C Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the ''PPP4C'' gene. Interactions PPP4C has been shown to interact with: * CCDC6, * CCT2, * CCT3, * CCT4, * CCT5, * CCT6A, * CCT7, * IG .... References External links * Further reading * * * * * * * * * {{gene-7-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CCT4
T-complex protein 1 subunit delta is a protein that in humans is encoded by the ''CCT4'' gene. The CCT4 protein is a component of the TRiC complex. Interactions CCT4 has been shown to interact with PPP4C Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the ''PPP4C'' gene. Interactions PPP4C has been shown to interact with: * CCDC6, * CCT2, * CCT3, * CCT4, * CCT5, * CCT6A, * CCT7, * IG .... References External links * Further reading * * * * * * * * * * * {{gene-2-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
