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Chaperonine

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https://www.readbyqxmd.com/read/28108864/is-raf1-protein-from-synechocystis-sp-pcc-6803-really-needed-in-the-cyanobacterial-rubisco-assembly-process
#1
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
#2
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
#3
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 17, 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-%C3%AF-helix-rich-trimeric-protein
#4
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 40-100 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 16, 2017: Bioconjugate Chemistry
https://www.readbyqxmd.com/read/28069816/the-interaction-of-the-cd43-sialomucin-with-the-mycobacterium-tuberculosis-cpn60-2-chaperonin-mediates-macrophage-tnf-%C3%AE-production
#5
Alvaro Torres-Huerta, Tomas Villaseñor, Angel Flores-Alcantar, Cristina Parada, Estefanía Alemán-Navarro, Clara Espitia, Gustavo Pedraza-Alva, Yvonne Rosenstein
Mycobacterium tuberculosis is the causal agent of tuberculosis. TNF-α, TGF-β and 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 mycobacteria-macrophage contact. We report here that Cpn60.2 induces both THP-1 cells and bone marrow-derived macrophages (BMMs) to produce TNF-α and that this production is CD43 dependent...
January 9, 2017: Infection and Immunity
https://www.readbyqxmd.com/read/28067475/the-chaperonin-tric-forms-an-oligomeric-complex-in-the-malaria-parasite-cytosol
#6
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
#7
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
#8
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
#9
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
#10
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
#11
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
#12
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
#13
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
#14
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
#15
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
https://www.readbyqxmd.com/read/27892468/somatic-increase-of-cct8-mimics-proteostasis-of-human-pluripotent-stem-cells-and-extends-c-elegans-lifespan
#16
Alireza Noormohammadi, Amirabbas Khodakarami, Ricardo Gutierrez-Garcia, Hyun Ju Lee, Seda Koyuncu, Tim König, Christina Schindler, Isabel Saez, Azra Fatima, Christoph Dieterich, David Vilchez
Human embryonic stem cells can replicate indefinitely while maintaining their undifferentiated state and, therefore, are immortal in culture. This capacity may demand avoidance of any imbalance in protein homeostasis (proteostasis) that would otherwise compromise stem cell identity. Here we show that human pluripotent stem cells exhibit enhanced assembly of the TRiC/CCT complex, a chaperonin that facilitates the folding of 10% of the proteome. We find that ectopic expression of a single subunit (CCT8) is sufficient to increase TRiC/CCT assembly...
November 28, 2016: Nature Communications
https://www.readbyqxmd.com/read/27874025/beyond-antibodies-development-of-a-novel-protein-scaffold-based-on-human-chaperonin-10
#17
Abdulkarim M Alsultan, David Y Chin, Christopher B Howard, Christopher J de Bakker, Martina L Jones, Stephen M Mahler
Human Chaperonin 10 (hCpn10) was utilised as a novel scaffold for presenting peptides of therapeutic and diagnostic significance. Molecular dynamic simulations and protein sizing analyses identified a peptide linker (P1) optimal for the formation of the quarternary hCpn10 heptamer structure. hCpn10 scaffold displaying peptides targeting Factor VIIa (CE76-P1) and CD44 (CP7) were expressed in E. coli. Functional studies of CE76-P1 indicated nanomolar affinity for Factor VIIa (3 nM) similar to the E-76 peptide (6 nM), with undetectable binding to Factor X...
November 22, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27842496/proteomics-analysis-reveals-novel-host-molecular-mechanisms-associated-with-thermotherapy-of-ca-liberibacter-asiaticus-infected-citrus-plants
#18
Chika C Nwugo, Melissa S Doud, Yong-Ping Duan, Hong Lin
BACKGROUND: Citrus Huanglongbing (HLB), which is linked to the bacterial pathogen 'Ca. Liberibacter asiaticus' (Las), is the most devastating disease of citrus plants, and longer-term control measures via breeding or genetic engineering have been unwieldy because all cultivated citrus species are susceptible to the disease. However, the degree of susceptibility varies among citrus species, which has prompted efforts to identify potential Las resistance/tolerance-related genes in citrus plants for application in breeding or genetic engineering programs...
November 14, 2016: BMC Plant Biology
https://www.readbyqxmd.com/read/27836796/development-of-a-simplified-purification-method-for-a-novel-formaldehyde-dismutase-variant-from-pseudomonas-putida-j3
#19
Lisa Blaschke, Wenke Wagner, Christina Werkmeister, Marion Wild, Adrian Gihring, Steffen Rupp, Susanne Zibek
Formaldehyde dismutase (FDM) is a very interesting enzyme, due to the fact that it comprises an internal cofactor regeneration mechanism. The FDM, therefore, is able to catalyze redox reactions independent of exogenous cofactor addition, rendering the enzyme powerful for industrial applications. Currently, only one enzyme of this type has been characterized enzymatically. Furthermore, only one additional DNA-sequence with high homology to FDM has been published. In this work, we identified a new variant of a formaldehyde dismutase gene (fdm) in the Pseudomonas putida J3 strain...
January 10, 2017: Journal of Biotechnology
https://www.readbyqxmd.com/read/27836734/doxorubicin-anti-tumor-mechanisms-include-hsp60-post-translational-modifications-leading-to-the-hsp60-p53-complex-dissociation-and-instauration-of-replicative-senescence
#20
Antonella Marino Gammazza, Claudia Campanella, Rosario Barone, Celeste Caruso Bavisotto, Magdalena Gorska, Michal Wozniak, Francesco Carini, Francesco Cappello, Antonella D'Anneo, Marianna Lauricella, Giovanni Zummo, Everly Conway de Macario, Alberto J L Macario, Valentina Di Felice
The chaperone Hsp60 is pro-carcinogenic in certain tumor types by interfering with apoptosis and with tumor cell death. In these tumors, it is not yet known whether doxorubicin anti-tumor effects include a blockage of the pro-carcinogenic action of Hsp60. We found a doxorubicin dose-dependent viability reduction in a human lung mucoepidermoid cell line that was paralleled by the appearance of cell senescence markers. Concomitantly, intracellular Hsp60 levels decreased while its acetylation levels increased...
January 28, 2017: Cancer Letters
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