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Pesquisa : D08.811.277.040.025.142.750.750 [Categoria DeCS]
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  1 / 39 MEDLINE  
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[PMID]:24459061
[Au] Autor:Renggli K; Nussbaumer MG; Urbani R; Pfohl T; Bruns N
[Ad] Endereço:Department of Chemistry, University of Basel, Klingelbergstrasse 80, 4056 Basel (Switzerland).
[Ti] Título:A chaperonin as protein nanoreactor for atom-transfer radical polymerization.
[So] Source:Angew Chem Int Ed Engl;53(5):1443-7, 2014 Jan 27.
[Is] ISSN:1521-3773
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The group II chaperonin thermosome (THS) from the archaea Thermoplasma acidophilum is reported as nanoreactor for atom-transfer radical polymerization (ATRP). A copper catalyst was entrapped into the THS to confine the polymerization into this protein cage. THS possesses pores that are wide enough to release polymers into solution. The nanoreactor favorably influenced the polymerization of N-isopropyl acrylamide and poly(ethylene glycol)methylether acrylate. Narrowly dispersed polymers with polydispersity indices (PDIs) down to 1.06 were obtained in the protein nanoreactor, while control reactions with a globular protein-catalyst conjugate only yielded polymers with PDIs above 1.84.
[Mh] Termos MeSH primário: Chaperoninas/metabolismo
Radicais Livres/química
Nanotecnologia
Termossomos/metabolismo
[Mh] Termos MeSH secundário: Acrilamidas/química
Acrilamidas/metabolismo
Catálise
Chaperoninas/química
Cobre/química
Ligantes
Poliaminas/química
Poliaminas/metabolismo
Polimerização
Thermoplasma/metabolismo
Termossomos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acrylamides); 0 (Free Radicals); 0 (Ligands); 0 (Polyamines); 03K6SX4V2J (diethylenetriamine); 789U1901C5 (Copper); B7GFF17L9U (N-isopropylacrylamide); EC 3.6.1.- (Chaperonins); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:140124
[Lr] Data última revisão:
140124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140125
[St] Status:MEDLINE
[do] DOI:10.1002/anie.201306798


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[PMID]:23709365
[Au] Autor:Zhang K; Wang L; Liu Y; Chan KY; Pang X; Schulten K; Dong Z; Sun F
[Ad] Endereço:National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
[Ti] Título:Flexible interwoven termini determine the thermal stability of thermosomes.
[So] Source:Protein Cell;4(6):432-44, 2013 Jun.
[Is] ISSN:1674-8018
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-ß), also called thermosomes, from Acidianus tengchongensis and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-ß is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αß is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-ß revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.
[Mh] Termos MeSH primário: Termossomos/metabolismo
[Mh] Termos MeSH secundário: Acidianus/metabolismo
Trifosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Microscopia Crioeletrônica
Concentração de Íons de Hidrogênio
Dados de Sequência Molecular
Mutação
Nucleotídeos/metabolismo
Ligação Proteica
Dobramento de Proteína
Estabilidade Proteica
Estrutura Quaternária de Proteína
Alinhamento de Sequência
Eletricidade Estática
Temperatura Ambiente
Termossomos/química
Termossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Nucleotides); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130528
[St] Status:MEDLINE
[do] DOI:10.1007/s13238-013-3026-9


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[PMID]:22995501
[Au] Autor:Jayasinghe M; Shrestha P; Wu X; Tehver R; Stan G
[Ad] Endereço:Department of Chemistry, Northern Kentucky University, Highland Heights, Kentucky, USA.
[Ti] Título:Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis.
[So] Source:Biophys J;103(6):1285-95, 2012 Sep 19.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chaperonins are molecular machines that use ATP-driven cycles to assist misfolded substrate proteins to reach the native state. During the functional cycle, these machines adopt distinct nucleotide-dependent conformational states, which reflect large-scale allosteric changes in individual subunits. Distinct allosteric kinetics has been described for the two chaperonin classes. Bacterial (group I) chaperonins, such as GroEL, undergo concerted subunit motions within each ring, whereas archaeal and eukaryotic chaperonins (group II) undergo sequential subunit motions. We study these distinct mechanisms through a comparative normal mode analysis of monomer and double-ring structures of the archaeal chaperonin thermosome and GroEL. We find that thermosome monomers of each type exhibit common low-frequency behavior of normal modes. The observed distinct higher-frequency modes are attributed to functional specialization of these subunit types. The thermosome double-ring structure has larger contribution from higher-frequency modes, as it is found in the GroEL case. We find that long-range intersubunit correlation of amino-acid pairs is weaker in the thermosome ring than in GroEL. Overall, our results indicate that distinct allosteric behavior of the two chaperonin classes originates from different wiring of individual subunits as well as of the intersubunit communications.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Modelos Moleculares
Termossomos/química
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Regulação Alostérica
Proteínas Arqueais/metabolismo
Mathanococcus
Movimento
Estrutura Terciária de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Termossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Protein Subunits); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120922
[St] Status:MEDLINE


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[PMID]:22584152
[Au] Autor:Han BG; Walton RW; Song A; Hwu P; Stubbs MT; Yannone SM; Arbeláez P; Dong M; Glaeser RM
[Ad] Endereço:Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720, USA.
[Ti] Título:Electron microscopy of biotinylated protein complexes bound to streptavidin monolayer crystals.
[So] Source:J Struct Biol;180(1):249-53, 2012 Oct.
[Is] ISSN:1095-8657
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chemical biotinylation of protein complexes followed by binding to two-dimensional (monolayer) crystals of streptavidin is shown to be an effective way to prepare cryo-EM specimens from samples at low protein concentration. Three different multiprotein complexes are used to demonstrate the generality of this method. In addition, native thermosomes, purified from Sulfolobus solfataricus P2, are used to demonstrate that a uniform distribution of Euler angles is produced, even though this particle is known to adopt a preferred orientation when other methods of cryo-EM specimen preparation are used.
[Mh] Termos MeSH primário: Biotina/química
Microscopia Crioeletrônica/métodos
Estreptavidina/química
[Mh] Termos MeSH secundário: Adsorção
Animais
Apoferritinas/química
Apoferritinas/ultraestrutura
Proteínas de Bactérias/química
Biotinilação
Cristalização
Desulfovibrio vulgaris
Cavalos
Modelos Moleculares
Complexos Multienzimáticos/química
Complexos Multienzimáticos/ultraestrutura
Ligação Proteica
Estrutura Quaternária de Proteína
Sulfolobus solfataricus
Termossomos/química
Termossomos/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Multienzyme Complexes); 6SO6U10H04 (Biotin); 89287-46-7 (6,7-dimethyl-8-ribityllumazine synthase); 9013-20-1 (Streptavidin); 9013-31-4 (Apoferritins); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120516
[St] Status:MEDLINE


  5 / 39 MEDLINE  
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[PMID]:21678771
[Au] Autor:Bruns N; Clark DS
[Ad] Endereço:Department of Chemistry, University of Basel, Klingelbergstr. 80, CH-4056 Basel. nico.bruns@unibas.ch
[Ti] Título:Self-reporting materials: protein-mediated visual indication of damage in a bulk polymer.
[So] Source:Chimia (Aarau);65(4):245-9, 2011.
[Is] ISSN:0009-4293
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Damage self-reporting materials are able to indicate the presence of microscopic damaged regions by easy to detect signals, such as fluorescence. Therefore, these smart materials can reduce the risk of catastrophic failure of load-bearing components, e.g., in aerospace and construction applications. We highlight here our proof-of-concept paper and we present some additional data, which shows that proteins can be used as mechanophores in solid polymeric materials. Macroscopic mechanical forces were transferred from the polymer to the embedded proteins. The biomolecules act as molecular strain sensor, giving the material the desired self-reporting property. Poly(ethylene glycol) and poly(acrylamide) (PAAm) networks were doped with small amounts of thermsosome (THS), a protein cage from the family of chaperonins, that encapsulated a pair of fluorescent proteins. THS acts as a scaffold which brings the two fluorescent proteins into distance suitable for fluorescence resonance energy transfer (FRET). Moreover, THS can be distorted by mechanic forces so that the distance between the fluorescent proteins changes, leading to a change in FRET efficiency. Using the brittle PAAm as a model system, we were able to visualize microcracks in the polymers by FRET microscopy and by fluorescence lifetime imaging. THS also stabilizes the encapsulated guest proteins against thermal denaturation, increasing their half-live at 70 degrees C by a factor of 2.3.
[Mh] Termos MeSH primário: Resinas Acrílicas/química
Proteínas de Bactérias/química
Proteínas de Fluorescência Verde/química
Proteínas Luminescentes/química
Polietilenoglicóis/química
Termossomos/metabolismo
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Microscopia de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Acrylic Resins); 0 (Bacterial Proteins); 0 (Cyan Fluorescent Protein); 0 (Luminescent Proteins); 0 (yellow fluorescent protein, Bacteria); 147336-22-9 (Green Fluorescent Proteins); 30IQX730WE (Polyethylene Glycols); 9003-05-8 (polyacrylamide); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1108
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110618
[St] Status:MEDLINE


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[PMID]:21265753
[Au] Autor:Lund P
[Ad] Endereço:School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK. lundpa@gmail.com
[Ti] Título:Insights into chaperonin function from studies on archaeal thermosomes.
[So] Source:Biochem Soc Trans;39(1):94-8, 2011 Jan.
[Is] ISSN:1470-8752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:It is now well understood that, although proteins fold spontaneously (in a thermodynamic sense), many nevertheless require the assistance of helpers called molecular chaperones to reach their correct and active folded state in living cells. This is because the pathways of protein folding are full of traps for the unwary: the forces that drive proteins into their folded states can also drive them into insoluble aggregates, and, particularly when cells are stressed, this can lead, without prevention or correction, to cell death. The chaperonins are a family of molecular chaperones, practically ubiquitous in all living organisms, which possess a remarkable structure and mechanism of action. They act as nanoboxes in which proteins can fold, isolated from their environment and from other partners with which they might, with potentially deleterious consequences, interact. The opening and closing of these boxes is timed by the binding and hydrolysis of ATP. The chaperonins which are found in bacteria are extremely well characterized, and, although those found in archaea (also known as thermosomes) and eukaryotes have received less attention, our understanding of these proteins is constantly improving. This short review will summarize what we know about chaperonin function in the cell from studies on the archaeal chaperonins, and show how recent work is improving our understanding of this essential class of molecular chaperones.
[Mh] Termos MeSH primário: Archaea/metabolismo
Chaperoninas/metabolismo
Termossomos/metabolismo
[Mh] Termos MeSH secundário: Chaperoninas/química
Chaperoninas/genética
Microscopia Crioeletrônica
Modelos Moleculares
Chaperonas Moleculares/química
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Conformação Proteica
Dobramento de Proteína
Termossomos/química
Termossomos/genética
Termossomos/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Molecular Chaperones); EC 3.6.1.- (Chaperonins); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1104
[Cu] Atualização por classe:161203
[Lr] Data última revisão:
161203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110127
[St] Status:MEDLINE
[do] DOI:10.1042/BST0390094


  7 / 39 MEDLINE  
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[PMID]:20719249
[Au] Autor:Stölken M; Beck F; Haller T; Hegerl R; Gutsche I; Carazo JM; Baumeister W; Scheres SH; Nickell S
[Ad] Endereço:Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
[Ti] Título:Maximum likelihood based classification of electron tomographic data.
[So] Source:J Struct Biol;173(1):77-85, 2011 Jan.
[Is] ISSN:1095-8657
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Classification and averaging of sub-tomograms can improve the fidelity and resolution of structures obtained by electron tomography. Here we present a three-dimensional (3D) maximum likelihood algorithm--MLTOMO--which is characterized by integrating 3D alignment and classification into a single, unified processing step. The novelty of our approach lies in the way we calculate the probability of observing an individual sub-tomogram for a given reference structure. We assume that the reference structure is affected by a 'compound wedge', resulting from the summation of many individual missing wedges in distinct orientations. The distance metric underlying our probability calculations effectively down-weights Fourier components that are observed less frequently. Simulations demonstrate that MLTOMO clearly outperforms the 'constrained correlation' approach and has advantages over existing approaches in cases where the sub-tomograms adopt preferred orientations. Application of our approach to cryo-electron tomographic data of ice-embedded thermosomes revealed distinct conformations that are in good agreement with results obtained by previous single particle studies.
[Mh] Termos MeSH primário: Algoritmos
Interpretação Estatística de Dados
Tomografia com Microscopia Eletrônica/métodos
Tomografia com Microscopia Eletrônica/estatística & dados numéricos
Modelos Moleculares
Termossomos/química
[Mh] Termos MeSH secundário: Tomografia com Microscopia Eletrônica/classificação
Funções Verossimilhança
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1103
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100820
[St] Status:MEDLINE
[do] DOI:10.1016/j.jsb.2010.08.005


  8 / 39 MEDLINE  
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[PMID]:20947016
[Au] Autor:Huo Y; Hu Z; Zhang K; Wang L; Zhai Y; Zhou Q; Lander G; Zhu J; He Y; Pang X; Xu W; Bartlam M; Dong Z; Sun F
[Ad] Endereço:National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
[Ti] Título:Crystal structure of group II chaperonin in the open state.
[So] Source:Structure;18(10):1270-9, 2010 Oct 13.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thermosomes are group II chaperonins responsible for protein refolding in an ATP-dependent manner. Little is known regarding the conformational changes of thermosomes during their functional cycle due to a lack of high-resolution structure in the open state. Here, we report the first complete crystal structure of thermosome (rATcpnß) in the open state from Acidianus tengchongensis. There is a ∼30° rotation of the apical and lid domains compared with the previous closed structure. Besides, the structure reveals a conspicuous hydrophobic patch in the lid domain, and residues locating in this patch are conserved across species. Both the closed and open forms of rATcpnß were also reconstructed by electron microscopy (EM). Structural fitting revealed the detailed conformational change from the open to the closed state. Structural comparison as well as protease K digestion indicated only ATP binding without hydrolysis does not induce chamber closure of thermosome.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Conformação Proteica
Termossomos/química
[Mh] Termos MeSH secundário: Acidianus/metabolismo
Difosfato de Adenosina/química
Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/química
Trifosfato de Adenosina/metabolismo
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Clonagem Molecular
Microscopia Crioeletrônica
Cristalização
Eletroforese em Gel de Poliacrilamida
Modelos Moleculares
Ligação Proteica
Dobramento de Proteína
Estrutura Terciária de Proteína
Termossomos/genética
Termossomos/metabolismo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1103
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101016
[St] Status:MEDLINE
[do] DOI:10.1016/j.str.2010.07.009


  9 / 39 MEDLINE  
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[PMID]:20117082
[Au] Autor:Wang L; Hu ZJ; Luo YM; Huo YW; Ma Q; He YZ; Zhang YY; Sun F; Dong ZY
[Ad] Endereço:Institute of Microbiology, Chinese Academy of Sciences, Beijing, PR China.
[Ti] Título:Distinct symmetry and limited peptide refolding activity of the thermosomes from the acidothermophilic archaea Acidianus tengchongensis S5(T).
[So] Source:Biochem Biophys Res Commun;393(2):228-34, 2010 Mar 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recombinant thermosomes from the Acidianus tengchongensis strain S5(T) were purified to homogeneity and assembled in vitro into homo-oligomers (rATcpnalpha or rATcpnbeta) and hetero-oligomers (rATcpnalphabeta). The symmetries of these complexes were determined by electron microscopy and image analysis. The rATcpnalpha homo-oligomer was shown to possess 8-fold symmetry while both rATcpnbeta and rATcpnalphabeta oligomers adopted 9-fold symmetry. rATcpnalphabeta oligomers were shown to contain the alpha and beta subunits in a 1:2 ratio. All of the complexes prevented the irreversible inactivation of yeast alcohol dehydrogenase at 55 degrees C and completely prevented the formation of aggregates during thermal inactivation of citrate synthase at 45 degrees C. All rATcpn complexes showed trace ATP hydrolysis activity. Furthermore, rATcpnbeta sequestered fully chemically denatured substrates (GFP and thermophilic malic dehydrogenase) in vitro without refolding them in an ATP-dependent manner. This property is similar to previously reported properties of chaperonins from Sulfolobus tokodaii and Sulfolobus acidocaldarius. These features are consistent with the slow growth rates of these species of archaea in their native environment.
[Mh] Termos MeSH primário: Acidianus/metabolismo
Peptídeos/metabolismo
Termossomos/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Hidrólise
Microscopia Eletrônica
Peptídeos/química
Peptídeos/genética
Filogenia
Dobramento de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sulfolobus/metabolismo
Sulfolobus acidocaldarius/metabolismo
Termossomos/química
Termossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 0 (Protein Subunits); 0 (Recombinant Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1003
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100202
[St] Status:MEDLINE
[do] DOI:10.1016/j.bbrc.2010.01.106


  10 / 39 MEDLINE  
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[PMID]:19908377
[Au] Autor:Kalisman N; Levitt M
[Ad] Endereço:Department of Structural biology, School of Medicine, Stanford University, Stanford, California 94305, USA.
[Ti] Título:Insights into the intra-ring subunit order of TRiC/CCT: a structural and evolutionary analysis.
[So] Source:Pac Symp Biocomput;:252-9, 2010.
[Is] ISSN:2335-6936
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:TRiC is an important group II chaperonin that facilitates the folding of many eukaryotic proteins. The TRiC complex consists of two stacked rings, each comprised of eight paralogous subunits with a mutual sequence identity of 30-35%. Each subunit has unique functional roles that are manifested by corresponding sequence conservation. It is generally assumed that the subunit order within each ring is fixed, but this order is still uncertain. Here we address the problem of the intra-ring subunit order by combining two sources of information: evolutionary conservation and a structural hypothesis. Specifically, we identify residues in the TRiC subunits that are likely to be part of the intra-unit interface, based on homology modeling to the solved thermosome structure. Within this set of residues, we search for a subset that shows an evolutionary conservation pattern that is indicative of the subunit order key. This pattern shows considerable conservation across species, but large variation across the eight subunits. By this approach we were able to locate two parts of the interface where complementary interactions seem to favor certain pairing of subunits. This knowledge leads to restrictions on the 5,040 (=7!) possible subunits arrangements in the ring, and limits them to just 72. Although our findings give only partial understanding of the inter-subunit interactions that determine their order, we conclude that they are comprised of complementary charged, polar and hydrophobic interactions that occur in both the equatorial and middle domains of each subunit.
[Mh] Termos MeSH primário: Chaperonina com TCP-1/química
Chaperonina com TCP-1/genética
[Mh] Termos MeSH secundário: Animais
Biologia Computacional
Sequência Conservada
Evolução Molecular
Seres Humanos
Modelos Moleculares
Domínios e Motivos de Interação entre Proteínas
Estrutura Quaternária de Proteína
Subunidades Proteicas
Homologia de Sequência de Aminoácidos
Homologia Estrutural de Proteína
Termossomos/química
Termossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Subunits); EC 3.6.1.- (Chaperonin Containing TCP-1); EC 3.6.1.- (Thermosomes)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091113
[St] Status:MEDLINE



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