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Chaperonine

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https://www.readbyqxmd.com/read/27908246/inhibition-of-chaperonin-groel-by-a-monomer-of-ovine-prion-protein-and-its-oligomeric-forms
#1
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
#2
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
#3
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
#4
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
#5
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...
November 9, 2016: 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
#6
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...
November 9, 2016: Cancer Letters
https://www.readbyqxmd.com/read/27810573/a-survey-of-coarse-grained-methods-for-modeling-protein-conformational-transitions
#7
REVIEW
Wenjun Zheng, Han Wen
The decryption of transient structural changes during protein conformational transitions is essential to a detailed understanding of protein functions. To this end, coarse-grained protein structural models have proven valuable by enabling cost-effective simulation/analysis of protein conformational transitions which are too slow for all-atom molecular dynamics simulation. Here we survey state-of-the-art coarse-grained methods for protein conformational transition modeling developed in the past decade, with focus on those available online to public...
October 27, 2016: Current Opinion in Structural Biology
https://www.readbyqxmd.com/read/27806916/functional-profiling-of-asymmetrically-organized-human-cct-tric-chaperonin
#8
Kazutaka Araki, Atsushi Suenaga, Hidewo Kusano, Riko Tanaka, Tomohisa Hatta, Tohru Natsume, Kazuhiko Fukui
Molecular organization of the eukaryote chaperonin known as CCT/TRiC complex was recently clarified. Eight distinct subunits are uniquely organized, providing a favorable folding cavity for specific client proteins such as tubulin and actin. Because of its heterogeneous subunit composition, CCT complex has polarized inner faces, which may underlie an essential part of its chaperonin function. In this study, we structurally characterized the closed and open states of CCT complex, using molecular dynamics analyses...
October 30, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27798950/comparative-proteome-analysis-of-xanthomonas-citri-subsp-citri-periplasmic-proteins-reveals-changes-in-cellular-envelope-metabolism-during-in-vitro-pathogenicity-induction
#9
Juliana Artier, Flávia da Silva Zandonadi, Flávia Maria de Souza Carvalho, Bianca Alves Pauletti, Adriana Franco Paes Leme, Carolina Moretto Carnielli, Heloisa Sobreiro Selistre de Araujo, Maria Célia Bertolini, Jesus Aparecido Ferro, José Belasque Júnior, Julio Cezar Franco de Oliveira, Maria Teresa Marques Novo-Mansur
Citrus canker is a plant disease caused by gram-negative bacteria from the genus Xanthomonas, and the most virulent species is Xanthomonas citri subsp.citri (XAC), which attacks a wide range of citrus hosts. Differential proteomic analysis of periplasm-enriched fraction was performed for XAC cells grown in pathogenicity-inducing (XAM-M) and pathogenicity non-inducing (NB) media, using two-dimensional electrophoresis combined with liquid chromatography-tandem mass spectrometry. Among the 40 proteins identified, transglycosylase was detected in a highly abundant spot in XAC cells grown under inducing condition...
October 31, 2016: Molecular Plant Pathology
https://www.readbyqxmd.com/read/27775711/staggered-atp-binding-mechanism-of-eukaryotic-chaperonin-tric-cct-revealed-through-high-resolution-cryo-em
#10
Yunxiang Zang, Mingliang Jin, Huping Wang, Zhicheng Cui, Liangliang Kong, Caixuan Liu, Yao Cong
The eukaryotic chaperonin TRiC (or CCT) assists in the folding of 10% of cytosolic proteins. Here we present two cryo-EM structures of Saccharomyces cerevisiae TRiC in a newly identified nucleotide partially preloaded (NPP) state and in the ATP-bound state, at 4.7-Å and 4.6-Å resolution, respectively. Through inner-subunit eGFP tagging, we identified the subunit locations in open-state TRiC and found that the CCT2 subunit pair forms an unexpected Z shape. ATP binding induces a dramatic conformational change on the CCT2 side, thereby suggesting that CCT2 plays an essential role in TRiC allosteric cooperativity...
October 24, 2016: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/27774450/effects-of-a-mutation-in-the-hspe1-gene-encoding-the-mitochondrial-co-chaperonin-hsp10-and-its-potential-association-with-a-neurological-and-developmental-disorder
#11
Anne S Bie, Paula Fernandez-Guerra, Rune I D Birkler, Shahar Nisemblat, Dita Pelnena, Xinping Lu, Joshua L Deignan, Hane Lee, Naghmeh Dorrani, Thomas J Corydon, Johan Palmfeldt, Liga Bivina, Abdussalam Azem, Kristin Herman, Peter Bross
We here report molecular investigations of a missense mutation in the HSPE1 gene encoding the HSP10 subunit of the HSP60/ HSP10 chaperonin complex that assists protein folding in the mitochondrial matrix. The mutation was identified in an infant who came to clinical attention due to infantile spasms at 3 months of age. Clinical exome sequencing revealed heterozygosity for a HSPE1 NM_002157.2:c.217C>T de novo mutation causing replacement of leucine with phenylalanine at position 73 of the HSP10 protein. This variation has never been observed in public exome sequencing databases or the literature...
2016: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/27771745/stress-responses-of-acinetobacter-strain-y-during-phenol-degradation
#12
Johnson Lin
Quantification of gene expression of Acinetobacter strain Y under 1000 mg/l of phenol was investigated using qPCR and proteomic analyses. The results show that Acinetobacter strain Y utilized 100 % of phenol within 18 h of exposure. The results of qPCR and proteomic analyses demonstrate a sequential expression of phenol-degrading genes of Acinetobacter strain Y via the ortho-pathway followed by the β-ketoadipate pathway. Many stress-responsive proteins such as chaperones, chaperonins, porins and the enzymes involved in the signal transduction pathway were upregulated especially in the early stage...
October 22, 2016: Archives of Microbiology
https://www.readbyqxmd.com/read/27754336/microcystin-bound-protein-patterns-in-different-cultures-of-microcystis-aeruginosa-and-field-samples
#13
Nian Wei, Lili Hu, Lirong Song, Nanqin Gan
Micocystin (MC) exists in Microcystis cells in two different forms, free and protein-bound. We examined the dynamic change in extracellular free MCs, intracellular free MCs and protein-bound MCs in both batch cultures and semi-continuous cultures, using high performance liquid chromatography and Western blot. The results showed that the free MC per cell remained constant, while the quantity of protein-bound MCs increased with the growth of Microcystis cells in both kinds of culture. Significant changes in the dominant MC-bound proteins occurred in the late exponential growth phase of batch cultures, while the dominant MC-bound proteins in semi-continuous cultures remained the same...
October 12, 2016: Toxins
https://www.readbyqxmd.com/read/27742838/modulating-the-effects-of-the-bacterial-chaperonin-groel-on-fibrillogenic-polypeptides-through-modification-of-domain-hinge-architecture
#14
Naoya Fukui, Kiho Araki, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
The isolated apical domain of the Escherichia coli GroEL subunit displays the ability to suppress the irreversible fibrillation of numerous amyloid-forming polypeptides. In previous experiments, we have shown that mutating Gly-192 (located at hinge II that connects the apical domain and the intermediate domain) to a tryptophan results in an inactive chaperonin whose apical domain is disoriented. In this study, we have utilized this disruptive effect of Gly-192 mutation to our advantage, by substituting this residue with amino acid residues of varying van der Waals volumes with the intent to modulate the affinity of GroEL toward fibrillogenic peptides...
November 25, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27722468/steric-confinement-and-enhanced-local-flexibility-assist-knotting-in-simple-models-of-protein-folding
#15
Miguel A Soler, Antonio Rey, Patrícia F N Faísca
The chaperonin complex GroEL-GroES is able to accelerate the folding process of knotted proteins considerably. However, the folding mechanism inside the chaperonin cage is elusive. Here we use a combination of lattice and off-lattice Monte Carlo simulations of simple Gō models to study the effect of physical confinement and local flexibility on the folding process of protein model systems embedding a trefoil knot in their native structure. This study predicts that steric confinement plays a specific role in the folding of knotted proteins by increasing the knotting probability for very high degrees of confinement...
September 29, 2016: Physical Chemistry Chemical Physics: PCCP
https://www.readbyqxmd.com/read/27720295/targeting-the-hsp60-10-chaperonin-systems-of-trypanosoma-brucei-as-a-strategy-for-treating-african-sleeping-sickness
#16
Sanofar Abdeen, Nilshad Salim, Najiba Mammadova, Corey M Summers, Karen Goldsmith-Pestana, Diane McMahon-Pratt, Peter G Schultz, Arthur L Horwich, Eli Chapman, Steven M Johnson
Trypanosoma brucei are protozoan parasites that cause African sleeping sickness in humans (also known as Human African Trypanosomiasis-HAT). Without treatment, T. brucei infections are fatal. There is an urgent need for new therapeutic strategies as current drugs are toxic, have complex treatment regimens, and are becoming less effective owing to rising antibiotic resistance in parasites. We hypothesize that targeting the HSP60/10 chaperonin systems in T. brucei is a viable anti-trypanosomal strategy as parasites rely on these stress response elements for their development and survival...
September 22, 2016: Bioorganic & Medicinal Chemistry Letters
https://www.readbyqxmd.com/read/27708139/regulation-of-gpcr-expression-through-an-interaction-with-cct7-a-subunit-of-the-cct-tric-complex
#17
Samuel Génier, Jade Degrandmaison, Pierrick Moreau, Pascale Labrecque, Terence E Hébert, Jean-Luc Parent
Mechanisms that prevent aggregation and promote folding of nascent G protein-coupled receptors (GPCRs) remain poorly understood. We identified chaperonin containing TCP-1 subunit eta (CCT7) as an interacting partner of the β-isoform of thromboxane A2 receptor (TPβ) by yeast two-hybrid screening. CCT7 coimmunoprecipitated with overexpressed TPβ and β2-adrenergic receptor (β2AR) in HEK 293 cells, but also with endogenous β2AR. CCT7 depletion by small interfering RNA reduced total and cell-surface expression of both receptors and caused redistribution of the receptors to juxtanuclear aggresomes, significantly more so for TPβ than β2AR...
December 1, 2016: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/27702574/cell-free-analysis-of-polyq-dependent-protein-aggregation-and-its-inhibition-by-chaperone-proteins
#18
Kodai Machida, Tomoaki Shigeta, Ayano Kobayashi, Ai Masumoto, Yuna Hidaka, Hiroaki Imataka
Protein misfolding and aggregation is one of the major causes of neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease and Huntington's disease. So far protein aggregation related to these diseases has been studied using animals, cultured cells or purified proteins. In this study, we show that a newly synthesized polyglutamine protein implicated in Huntington's disease forms large aggregates in HeLa cells, and successfully recapitulate the process of this aggregation using a translation-based system derived from HeLa cell extracts...
October 1, 2016: Journal of Biotechnology
https://www.readbyqxmd.com/read/27686496/transient-kinetic-analysis-of-atp-hydrolysis-by-the-cct-tric-chaperonin
#19
Ilia Korobko, Michal Nadler-Holly, Amnon Horovitz
The chaperonin-containing t-complex polypeptide 1 (CCT, also known as TRiC) assists protein folding in an ATP-dependent manner. CCT/TRiC was mixed rapidly with different concentrations of ATP, and the amount of phosphate formed upon ATP hydrolysis was measured as a function of time using the coumarin-labeled phosphate-binding protein method. Two burst phases were observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis. The phases were assigned by (i) determining their dependence on ATP and K(+) concentrations and (ii) by measuring their sensitivity to the mutation Gly345→Asp in subunit CCT4, which decreases cooperativity in ATP binding...
September 26, 2016: Journal of Molecular Biology
https://www.readbyqxmd.com/read/27678307/quantitative-proteomics-reveals-the-defense-response-of-wheat-against-puccinia-striiformis-f-sp-tritici
#20
Yuheng Yang, Yang Yu, Chaowei Bi, Zhensheng Kang
Wheat stripe rust, caused by Puccinia striiformis f. sp. tritici (Pst), is considered one of the most aggressive diseases to wheat production. In this study, we used an iTRAQ-based approach for the quantitative proteomic comparison of the incompatible Pst race CYR23 in infected and non-infected leaves of the wheat cultivar Suwon11. A total of 3,475 unique proteins were identified from three key stages of interaction (12, 24, and 48 h post-inoculation) and control groups. Quantitative analysis showed that 530 proteins were differentially accumulated by Pst infection (fold changes >1...
September 28, 2016: Scientific Reports
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