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Chaperonine

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https://www.readbyqxmd.com/read/28178129/chaperonin-hsp60-and-annexin-2-are-candidate-biomarkers-for-non-small-cell-lung-carcinoma
#1
İsmail Ağababaoğlu, Ahmet Önen, Ayşe Banu Demir, Safiye Aktaş, Zekiye Altun, Hasan Ersöz, Aydn Şanl, Nezih Özdemir, Atila Akkoçlu
BACKGROUND: Lung cancer is responsible of 12.4% and 17.6% of all newly diagnosed cancer cases and mortality due to cancer, respectively, and 5-year survival rate despite all improved treatment options is 15%. This survival rate reaches 66% in the Stage 1 and surgically treated patients. Early diagnosis which could not be definitely and commonly achieved yet is extremely critical in obtaining high survival rate in this disease. For this reason; proteomic differences were evaluated using matrix assisted laser desorption ionization (MALDI) mass spectrometry in the subgroups of lung adenocarcinoma and squamous cell carcinoma...
February 2017: Medicine (Baltimore)
https://www.readbyqxmd.com/read/28156097/confinement-and-stabilization-of-fyn-sh3-folding-intermediate-mimetics-within-the-cavity-of-the-chaperonin-groel-demonstrated-by-relaxation-based-nmr
#2
David S Libich, Vitali Tugarinov, Rodolfo Ghirlando, G Marius Clore
The interaction of two folding intermediate mimetics of the model protein substrate Fyn SH3 with the chaperonin GroEL, a supramolecular foldase/unfoldase machine, has been investigated by (15)N relaxation-based nuclear magnetic resonance spectroscopy (lifetime line broadening, dark state exchange saturation transfer, and relaxation dispersion). The two mimetics comprise C-terminal truncations of wild-type and triple-mutant (A39V/N53P/V55L) Fyn SH3 in which the C-terminal strand of the SH3 domain is unfolded, while preserving the remaining domain structure...
February 8, 2017: Biochemistry
https://www.readbyqxmd.com/read/28143946/cellular-proteomes-drive-tissue-specific-regulation-of-the-heat-shock-response
#3
Jian Ma, Christopher E Grant, Rosemary N Plagens, Lindsey N Barrett, Karen S Kim Guisbert, Eric Guisbert
The heat shock response (HSR) is a cellular stress response that senses protein misfolding and restores protein folding homeostasis, or proteostasis. We previously identified an HSR regulatory network in Caenorhabditis elegans consisting of highly conserved genes that have important cellular roles in maintaining proteostasis. Unexpectedly, the effects of these genes on the heat shock response are distinctly tissue-specific. Here, we explore this apparent discrepancy and find that muscle-specific regulation of the HSR by the TRiC/CCT chaperonin is not driven by an enrichment of TRiC/CCT in muscle, but rather by the levels of one of its most abundant substrates, actin...
January 30, 2017: G3: Genes—Genomes—Genetics
https://www.readbyqxmd.com/read/28126905/a-trimer-consisting-of-the-tubulin-specific-chaperone-tbcd-regulatory-gtpase-arl2-and-%C3%AE-tubulin-is-required-for-maintaining-the-microtubule-network
#4
Joshua W Francis, Laura E Newman, Leslie A Cunningham, Richard A Kahn
Microtubule dynamics involves the polymerization and depolymerization of tubulin dimers and is an essential and highly regulated process required for cell viability, architecture, and division. The regulation of the microtubule network also depends upon the maintenance of a pool of αβ-tubulin heterodimers. These dimers are the end result a complex folding and assembly events, requiring the TriC/CCT chaperonin and five tubulin-specific chaperones, TBCA-E. However, models of the actions of these chaperones are incomplete or inconsistent...
January 26, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28125284/biogenesis-and-metabolic-maintenance-of-rubisco
#5
Andreas Bracher, Spencer M Whitney, F Ulrich Hartl, Manajit Hayer-Hartl
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) mediates the fixation of atmospheric CO2 in photosynthesis by catalyzing the carboxylation of the 5-carbon sugar ribulose-1,5-bisphosphate (RuBP). Rubisco is a remarkably inefficient enzyme, fixing only 2-10 CO2 molecules per second. Efforts to increase crop yields by bioengineering Rubisco remain unsuccessful, owing in part to the complex cellular machinery required for Rubisco biogenesis and metabolic maintenance. The large subunit of Rubisco requires the chaperonin system for folding, and recent studies have shown that assembly of hexadecameric Rubisco is mediated by specific assembly chaperones...
January 11, 2017: Annual Review of Plant Biology
https://www.readbyqxmd.com/read/28108864/is-raf1-protein-from-synechocystis-sp-pcc-6803-really-needed-in-the-cyanobacterial-rubisco-assembly-process
#6
Piotr Kolesinski, Malgorzata Rydzy, Andrzej Szczepaniak
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is responsible for carbon dioxide conversion during photosynthesis and, therefore, is the most important protein in biomass generation. Modifications of this biocatalyst toward improvements in its properties are hindered by the complicated and not yet fully understood assembly process required for the formation of active holoenzymes. An entire set of auxiliary factors, including chaperonin GroEL/GroES and assembly chaperones RbcX or Rubisco accumulation factor 1 (RAF1), is involved in the folding and subsequent assembly of Rubisco subunits...
January 20, 2017: Photosynthesis Research
https://www.readbyqxmd.com/read/28102321/the-chaperonin-cct-inhibits-assembly-of-%C3%AE-synuclein-amyloid-fibrils-by-a-specific-conformation-dependent-interaction
#7
Begoña Sot, Alejandra Rubio-Muñoz, Ahudrey Leal-Quintero, Javier Martínez-Sabando, Miguel Marcilla, Cintia Roodveldt, José M Valpuesta
The eukaryotic chaperonin CCT (chaperonin containing TCP-1) uses cavities built into its double-ring structure to encapsulate and to assist folding of a large subset of proteins. CCT can inhibit amyloid fibre assembly and toxicity of the polyQ extended mutant of huntingtin, the protein responsible for Huntington's disease. This raises the possibility that CCT modulates other amyloidopathies, a still-unaddressed question. We show here that CCT inhibits amyloid fibre assembly of α-synuclein A53T, one of the mutants responsible for Parkinson's disease...
January 19, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28096334/role-of-cct-chaperonin-in-the-disassembly-of-mitotic-checkpoint-complexes
#8
Sharon Kaisari, Danielle Sitry-Shevah, Shirly Miniowitz-Shemtov, Adar Teichner, Avram Hershko
The mitotic checkpoint system prevents premature separation of sister chromatids in mitosis and thus ensures the fidelity of chromosome segregation. When this checkpoint is active, a mitotic checkpoint complex (MCC), composed of the checkpoint proteins Mad2, BubR1, Bub3, and Cdc20, is assembled. MCC inhibits the ubiquitin ligase anaphase promoting complex/cyclosome (APC/C), whose action is necessary for anaphase initiation. When the checkpoint signal is turned off, MCC is disassembled, a process required for exit from checkpoint-arrested state...
January 31, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28090773/protein-nanoparticle-formation-using-a-circularly-permuted-%C3%AE-helix-rich-trimeric-protein
#9
Norifumi Kawakami, Hiroki Kondo, Masayuki Muramatsu, Kenji Miyamoto
We here report the production of highly spherical protein nanoparticles based on the domain-swapping oligomerization of a circularly permuted trimeric protein, major histocompatibility complex (MHC) class II associated chaperonin. The size distribution of the nanoparticles can be adjusted to between 40 and 100 nm in diameter, and thus, these particles are suitable as drug carriers following purification under basic conditions. Our approach involves no harsh treatments and could provide an alternative approach for protein nanoparticle formation...
January 20, 2017: Bioconjugate Chemistry
https://www.readbyqxmd.com/read/28069816/interaction-of-the-cd43-sialomucin-with-the-mycobacterium-tuberculosis-cpn60-2-chaperonin-leads-to-tumor-necrosis-factor-alpha-production
#10
Alvaro Torres-Huerta, Tomás Villaseñor, Angel Flores-Alcantar, Cristina Parada, Estefanía Alemán-Navarro, Clara Espitia, Gustavo Pedraza-Alva, Yvonne Rosenstein
Mycobacterium tuberculosis is the causal agent of tuberculosis. Tumor necrosis factor alpha (TNF-α), transforming growth factor β (TGF-β), and gamma interferon (IFN-γ) secreted by activated macrophages and lymphocytes are considered essential to contain Mycobacterium tuberculosis infection. The CD43 sialomucin has been reported to act as a receptor for bacilli through its interaction with the chaperonin Cpn60.2, facilitating mycobacterium-macrophage contact. We report here that Cpn60.2 induces both human THP-1 cells and mouse-derived bone marrow-derived macrophages (BMMs) to produce TNF-α and that this production is CD43 dependent...
March 2017: Infection and Immunity
https://www.readbyqxmd.com/read/28067475/the-chaperonin-tric-forms-an-oligomeric-complex-in-the-malaria-parasite-cytosol
#11
Natalie J Spillman, Josh R Beck, Suresh M Ganesan, Jacquin C Niles, Daniel E Goldberg
The malaria parasite exports numerous proteins into its host red blood cell (RBC). The trafficking of these exported effectors is complex. Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes...
January 9, 2017: Cellular Microbiology
https://www.readbyqxmd.com/read/28056218/neisseria-arctica-sp-nov-isolated-from-nonviable-eggs-of-greater-white-fronted-geese-anser-albifrons-in-arctic-alaska
#12
Cristina M Hansen, Elizabeth A Himschoot, Rebekah F Hare, Brandt W Meixell, Caroline Van Hemert, Karsten Hueffer
During the summers of 2013 and 2014, isolates of a novel Gram-negative coccus in the Neisseria genus were obtained from the contents of nonviable greater white-fronted goose (Anser albifrons) eggs on the Arctic Coastal Plain of Alaska. We used a polyphasic approach to determine whether these isolates represent a novel species. 16S rRNA gene sequences, 23S rRNA gene sequences, and chaperonin 60 gene sequences suggested that these Alaskan isolates are members of a distinct species that is most closely related to Neisseria canis, N...
January 5, 2017: International Journal of Systematic and Evolutionary Microbiology
https://www.readbyqxmd.com/read/28017766/folding-and-unfolding-pathway-of-chaperonin-groel-monomer-and-elucidation-of-thermodynamic-parameters
#13
Sarita Puri, Tapan K Chaudhuri
The conformation and thermodynamic stability of monomeric GroEL were studied by CD and fluorescence spectroscopy. GroEL denaturation with urea and dilution in buffer leads to formation of a folded GroEL monomer. The monomeric nature of this protein was verified by size-exclusion chromatography and native PAGE. It has a well-defined secondary and tertiary structure, folding activity (prevention of aggregation) for substrate protein and is resistant to proteolysis. Being a properly folded and reversibly refoldable, monomeric GroEL is amenable for the study of thermodynamic stability by unfolding transition methods...
December 23, 2016: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/28008398/dynamic-complexes-in-the-chaperonin-mediated-protein-folding-cycle
#14
REVIEW
Celeste Weiss, Fady Jebara, Shahar Nisemblat, Abdussalam Azem
The GroEL-GroES chaperonin system is probably one of the most studied chaperone systems at the level of the molecular mechanism. Since the first reports of a bacterial gene involved in phage morphogenesis in 1972, these proteins have stimulated intensive research for over 40 years. During this time, detailed structural and functional studies have yielded constantly evolving concepts of the chaperonin mechanism of action. Despite of almost three decades of research on this oligomeric protein, certain aspects of its function remain controversial...
2016: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28004338/network-analysis-identifies-disease-specific-pathways-for-parkinson-s-disease
#15
Chiara Monti, Ilaria Colugnat, Leonardo Lopiano, Adriano Chiò, Tiziana Alberio
Neurodegenerative diseases are characterized by the progressive loss of specific neurons in selected regions of the central nervous system. The main clinical manifestation (movement disorders, cognitive impairment, and/or psychiatric disturbances) depends on the neuron population being primarily affected. Parkinson's disease is a common movement disorder, whose etiology remains mostly unknown. Progressive loss of dopaminergic neurons in the substantia nigra causes an impairment of the motor control. Some of the pathogenetic mechanisms causing the progressive deterioration of these neurons are not specific for Parkinson's disease but are shared by other neurodegenerative diseases, like Alzheimer's disease and amyotrophic lateral sclerosis...
December 21, 2016: Molecular Neurobiology
https://www.readbyqxmd.com/read/27978916/-analysis-of-virulence-factors-of-porphyromonas-endodontalis-based-on-comparative-proteomics-technique
#16
H Li, H Ji, S S Wu, B X Hou
Objective: To analyze the protein expression profile and the potential virulence factors of Porphyromonas endodontalis (Pe) via comparison with that of two strains of Porphyromonas gingivalis (Pg) with high and low virulences, respectively. Methods: Whole cell comparative proteomics of Pe ATCC35406 was examined and compared with that of high virulent strain Pg W83 andlow virulent strain Pg ATCC33277, respectively. Isobaric tags for relative and absolute quantitation (iTRAQ) combined with nano liquid chromatography-tandem mass spectrometry (Nano-LC-MS/MS) were adopted to identify and quantitate the proteins of Pe and two strains of Pg with various virulences by using the methods of isotopically labeled peptides, mass spectrometric detection and bioinformatics analysis...
December 9, 2016: Zhonghua Kou Qiang Yi Xue za Zhi, Zhonghua Kouqiang Yixue Zazhi, Chinese Journal of Stomatology
https://www.readbyqxmd.com/read/27929117/cct-complex-restricts-neuropathogenic-protein-aggregation-via-autophagy
#17
Mariana Pavel, Sara Imarisio, Fiona M Menzies, Maria Jimenez-Sanchez, Farah H Siddiqi, Xiaoting Wu, Maurizio Renna, Cahir J O'Kane, Damian C Crowther, David C Rubinsztein
Aberrant protein aggregation is controlled by various chaperones, including CCT (chaperonin containing TCP-1)/TCP-1/TRiC. Mutated CCT4/5 subunits cause sensory neuropathy and CCT5 expression is decreased in Alzheimer's disease. Here, we show that CCT integrity is essential for autophagosome degradation in cells or Drosophila and this phenomenon is orchestrated by the actin cytoskeleton. When autophagic flux is reduced by compromise of individual CCT subunits, various disease-relevant autophagy substrates accumulate and aggregate...
December 8, 2016: Nature Communications
https://www.readbyqxmd.com/read/27924266/conformational-shift-in-the-closed-state-of-groel-induced-by-atp-binding-triggers-a-transition-to-the-open-state
#18
Yuka Suzuki, Kei Yura
We investigated the effect of ATP binding to GroEL and elucidated a role of ATP in the conformational change of GroEL. GroEL is a tetradecamer chaperonin that helps protein folding by undergoing a conformational change from a closed state to an open state. This conformational change requires ATP, but does not require the hydrolysis of the ATP. The following three types of conformations are crystalized and the atomic coordinates are available; closed state without ATP, closed state with ATP and open state with ADP...
2016: Biophysics and Physicobiology
https://www.readbyqxmd.com/read/27924258/chaperonin-groel-uses-asymmetric-and-symmetric-reaction-cycles-in-response-to-the-concentration-of-non-native-substrate-proteins
#19
REVIEW
Ryo Iizuka, Takashi Funatsu
The Escherichia coli chaperonin GroEL is an essential molecular chaperone that mediates protein folding in association with its cofactor, GroES. It is widely accepted that GroEL alternates the GroES-sealed folding-active rings during the reaction cycle. In other words, an asymmetric GroEL-GroES complex is formed during the cycle, whereas a symmetric GroEL-(GroES)2 complex is not formed. However, this conventional view has been challenged by the recent reports indicating that such symmetric complexes can be formed in the GroEL-GroES reaction cycle...
2016: Biophysics and Physicobiology
https://www.readbyqxmd.com/read/27908246/inhibition-of-chaperonin-groel-by-a-monomer-of-ovine-prion-protein-and-its-oligomeric-forms
#20
S S Kudryavtseva, Y Y Stroylova, I A Zanyatkin, T Haertle, V I Muronetz
The possibility of inhibition of chaperonin functional activity by amyloid proteins was studied. It was found that the ovine prion protein PrP as well as its oligomeric and fibrillar forms are capable of binding with the chaperonin GroEL. Besides, GroEL was shown to promote amyloid aggregation of the monomeric and oligomeric PrP as well as PrP fibrils. The monomeric PrP was shown to inhibit the GroEL-assisted reactivation of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The oligomers of PrP decelerate the GroEL-assisted reactivation of GAPDH, and PrP fibrils did not affect this process...
October 2016: Biochemistry. Biokhimii︠a︡
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