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GroES Protein (0):
Recent article
GroES Protein
Electrophoresis (30)6 2009
Abstract
The identification of cell components involved in probiotic activities is a challenge in current probiotic research. In this work, a new approach based on proteomics as an analytical tool for the identification of characteristic protein profiles related to adhesion to mucin as a model probiotic prop...
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PMID: 19309013
PDF is available here.
PDF is available here.
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Abstract
We demonstrate that the overexpression of the GroELS chaperone system, which assists the folding of intracellular proteins and prevents aggregation of its biological targets, can enhance the thermotolerance of Escherichia coli strains and facilitate the production of recombinant protein under therma...
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PMID: 19190411
PDF is available here.
PDF is available here.
Abstract
We described a high affinity interaction between GroES and two different 20 S (immuno- and constitutive) proteasomes, uncovering new scenarios on their possible physio-pathological role, specifically on the ability of proteasomes to interact both with unfolding and folding- assisting macromolecules....
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PMID: 19006106
PDF is available here.
PDF is available here.
ChemBioChem (9)18 2008
Abstract
Abstract
We focus on the bacterial GroE and DnaK systems, describe their temperature-sensitive protein components, and the location of the thermosensor within the structure of these components. While the thermosensor of the GroE system is located at the inter-ring interface of GroEL, that of the DnaK system...
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PMID: 19075746
PDF is available here.
PDF is available here.
Abstract
We observe that the difference is caused by reversible multimolecular association while folding in solution, an avenue of kinetic partitioning that slows the overall rate of renaturation relative to the chaperonin chamber, where such associations cannot occur. For Rubisco, reversible aggregation dur...
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PMID: 18987317
PDF is available here.
PDF is available here.
Abstract
We show that the hemicycle time (HCT) is determined by the mean residence time (MRT) of GroES on the cis ring of GroEL. In turn, this is governed by allosteric interactions within the trans ring of GroEL. Ligands that enhance the R (relaxed) state (residual ADP, the product of the previous hemicycle...
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PMID: 18988739
PDF is available here.
PDF is available here.
Abstract
The effects of potassium ion on the nested allostery of GroEL are due to increases in the affinity for nucleotide. Both positive allosteric transitions, TT-TR and TR-RR, occur at lower [ATP] as [K(+)] is increased. Negative cooperativity in the double-ringed system is also due to an increase in the...
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PMID: 18988745
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)46 2008
Abstract
We use a chemically modified mutant of GroEL (EL43Py) to uncouple substrate protein encapsulation from release and folding. Although EL43Py correctly initiates a substrate protein encapsulation reaction, this mutant stalls in an intermediate allosteric state of the GroEL ring, which is essential for...
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PMID: 18782766
PDF is available here.
PDF is available here.
Abstract
We use mass spectrometry to monitor the disassembly induced by thermal activation of the heptameric co-chaperonins GroES and gp31. We use native electrospray ionization mass spectrometry (ESI-MS) on a Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer to monitor the stoichiometry o...
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PMID: 18972453
PDF is available here.
PDF is available here.
Abstract
We combine all-atom molecular dynamics simulations with data from experimental assays of the activity of the bacterial chaperonin GroEL to demonstrate that a chaperonin's ability to facilitate folding is correlated with the affinity of its interior surface for water. Our results suggest a novel view...
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PMID: 18710231
PDF is available here.
PDF is available here.
Journal of Molecular Biology (381)3 2008
Abstract
We performed binding experiments with a peptide construct of the tail to establish its specificity for Aacpn10del-25 and used cryo-electron microscopy to determine the three-dimensional (3D) structure of the GroEL-Aacpn10-ADP complex at an 8-A resolution. We found that the GroEL-Aacpn10 structure is...
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PMID: 18588898
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)35 2008
Abstract
We monitored the GroEL-GroES interaction in the reaction cycle using fluorescence resonance energy transfer. We found that nearly equivalent amounts of symmetric GroEL-(GroES)(2) (football-shaped) complex and asymmetric GroEL-GroES (bullet-shaped) complex coexist during the functional reaction cycle...
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PMID: 18567585
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)35 2008
Abstract
We found that a substrate protein prebound to the trans-ring remained bound during the first ATP cycle, and this substrate was assisted by GroEL-GroES when the second cycle began. Moreover, a slow ATP-hydrolyzing GroEL mutant (D398A) in the ATP-bound form bound a substrate protein and GroES to the t...
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PMID: 18567584
PDF is available here.
PDF is available here.
Abstract
These results indicate that the novel ZMW makes feasible the direct observation of protein-protein interaction at an intracellular concentration in real time....
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PMID: 18563914
PDF is available here.
PDF is available here.
Atherosclerosis (199)1 2008
Abstract
We demonstrated these structures were of chlamydial origin. In the current study, we demonstrated the presence of aberrant bodies of C. pneumoniae in vivo in archival coronary atheromatous heart tissues by the immunogold electron microscopy technique....
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PMID: 18028932
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)26 2008
Abstract
We generated single polypeptide GroES by fusing seven subunits with various combinations of active and GroEL binding-defective subunits. Functional tests of the fused GroES variants indicated that four active GroES subunits were required for efficient formation of the stable GroEL/GroES complex and...
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PMID: 18430731
PDF is available here.
PDF is available here.
The Journal of Chemical Physics (128)23 2008
Abstract
Polar confinement induces an amorphous solidlike state of water characterized by an orientational correlation time longer than hundreds of picoseconds and significant structural disorder. Solvation behavior of methane molecules is dramatically modulated under polar confinement. Moreover our simulati...
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PMID: 18570509
PDF is available here.
PDF is available here.
Abstract
We considered, on a global scale, the relationship between the predicted fraction of protein disorder and the RNA and protein expression in Escherichia coli. Fraction of protein disorder correlated positively with both measured RNA expression levels of E. coli genes in three different growth media a...
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PMID: 18465893
PDF is available here.
PDF is available here.
Biochimica et Biophysica Acta (1784)6 2008
Abstract
We describe the behavior of an engineered, backbone-reversed form of the 97 residues-long GroES co-chaperonin of Escherichia coli. FTIR and far-UV CD spectroscopy suggest that retro-GroES adopts a mixed polyproline type II (PPII)-beta-strand structure with a beta(II) type CD spectrum similar to that...
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PMID: 18359305
PDF is available here.
PDF is available here.
EMBO Journal (27)10 2008
Abstract
We replaced wild-type GroEL with mutants of GroEL having either a reduced cage volume or altered charge properties of the cage wall. A stepwise reduction in cage size resulted in a gradual loss of cell viability, although the mutants bound non-native protein efficiently. Strikingly, a mild reduction...
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PMID: 18418386
PDF is available here.
PDF is available here.
Biophysical Journal (94)8 2008
Abstract
We probe the importance of the unfoldase nature of GroEL under conditions where aggregation is the predominant protein degradation pathway. We consider the effect of a hypothetical mutation to GroEL which increases the cycle frequency of GroEL/ES by increasing the rate of hydrolysis of GroEL-bound A...
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PMID: 18192377
PDF is available here.
PDF is available here.
Journal of Molecular Biology (377)5 2008
Abstract
We found that GroES formed a typical amyloid fibril from a guanidine hydrochloride (Gdn-HCl) unfolded state at neutral pH. Here, we report that other hsp10 homologues, such as human hsp10 (Hhsp10), rat mitochondrial hsp10 (Rhsp10), Gp31 from T4 phage, and hsp10 from the hyperthermophilic bacteria Th...
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PMID: 18329043
PDF is available here.
PDF is available here.
Abstract
The chaperone-like activity of a nanogel of cholesteryl group-bearing pullulan (CHP) was compared with that of GroEL for refolding acid-denatured green fluorescent protein (GFP). The refolding of denatured GFP was carried out by dilution of acid-denatured GFP in the presence of the nanogel or GroEL....
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PMID: 18179818
PDF is available here.
PDF is available here.
Abstract
We have expressed IRP1 using the plasmid pT7-His-hIRP1, which codifies for human IRP1 attached to an NH2-terminal 6-His tag. IRP1 was expressed in Escherichia coli using the strategy of co-expressing chaperonins GroES and GroEL, in order to circumvent inclusion body formation and increase the yield...
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PMID: 18297188
PDF is available here.
PDF is available here.
Abstract
We employed single molecule and ensemble FRET to monitor the conformational transitions of a model substrate as it proceeds along this chaperone pathway. We find that DnaK/DnaJ stabilizes the protein in collapsed states that fold exceedingly slowly. Transfer to GroEL results in unfolding, with a fra...
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PMID: 18394994
PDF is available here.
PDF is available here.
Journal of Medical Microbiology (57)Pt 4 2008
Abstract
The sequence diversity of groESL genes among Streptococcus bovis group isolates was analysed, including five reference strains and 36 clinical isolates. Phylogenetic analysis of the groES and groEL sequences showed that the isolates that belonged to the same species or subspecies usually clustered t...
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PMID: 18349361
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)14 2008
Abstract
We have found that GroEL1 from Chlamydophila pneumoniae, an obligate human pathogen, has a broader selectivity for nucleotides in the refolding reaction. To elucidate structural factors involved in such nucleotide selectivity, GroEL chimeras were constructed by exchanging apical, intermediate, and e...
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PMID: 18230606
PDF is available here.
PDF is available here.
Abstract
We employ single-particle electron cryo-microscopy (cryo-EM) to reconstruct GroEL to approximately 4 A resolution with both D7 and C7 symmetry. Using a newly developed skeletonization algorithm and secondary structure element identification in combination with sequence-based secondary structure pred...
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PMID: 18334219
PDF is available here.
PDF is available here.
Biophysical Journal (94)4 2008
Abstract
We studied the structure of the GroEL-GroES complex under physiological conditions by small-angle x-ray scattering, which is a powerful technique to directly observe the structure of the protein complex in solution. We evaluated molecular structural parameters, the radius of gyration and the maximum...
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PMID: 17981896
PDF is available here.
PDF is available here.
Abstract
We report a combination of atomistic and coarse-grained simulations that probe the structure and dynamics of the equatorial region of the GroEL/GroES chaperonin complex. Surprisingly, our simulations show that the equatorial region provides a translocation channel that will block the passage of fold...
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PMID: 18463703
PDF is available here.
PDF is available here.
Abstract
The results indicated that lowering the temperature, use of GroEL, GroES and glycerol could be few controlling factors for the solubilization of recombinant aggregation-prone maltodextrin glucosidase in E. coli. SIGNIFICANCE AND IMPACT OF THE STUDY: Our study could help in developing the strategy fo...
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PMID: 18171380
PDF is available here.
PDF is available here.
Abstract
In an attempt to investigate the molecular mechanism underlying human glucose-6-phosphate dehydrogenase (G6PD) deficiency caused by two mutations, G6PD(Plymouth) (G163D) and G6PD(Mahidol) (G163S), the two variants were constructed by site-directed mutagenesis and expressed in G6PD-deficient E. coli...
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PMID: 17959407
PDF is available here.
PDF is available here.
Protein & Peptide Letters (15)10 2008
Abstract
Expression of plant proteins in E. coli is frequently unsuccessful, but soluble and functional rice catalase-B can be produced in E. coli when it is co-expressed with the chaperone GroEL/ES. The rice catalase exhibited properties typical for a catalase including the decomposition of H(2)O(2) and inh...
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PMID: 19075818
PDF is available here.
PDF is available here.
Journal of Synchrotron Radiation (15)Pt 1 2008
Abstract
The resolution of X-ray diffraction microscopy is limited by the maximum dose that can be delivered prior to sample damage. In the proposed serial crystallography method, the damage problem is addressed by distributing the total dose over many identical hydrated macromolecules running continuously i...
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PMID: 18097080
PDF is available here.
PDF is available here.
Abstract
We have addressed this question by using NMR measurements of the time course of acquisition of amide proton exchange protection of human dihydrofolate reductase (DHFR) during folding in the presence of methotrexate and ATP either free in solution or inside the stable cavity formed between a single r...
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PMID: 18093916
PDF is available here.
PDF is available here.
Abstract
We have cloned the promoter containing region (P(g)) of groES-groEL operon of S. aureus Newman and found that the above promoter is induced by sublethal concentrations of many antibiotics including cell-wall active antibiotics. A reporter S. aureus RN4220 strain (designated SAU006) was constructed b...
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PMID: 18047789
PDF is available here.
PDF is available here.
Immunology (122)4 2007
Abstract
We reasoned that antigen/CD1 chimeras containing the different CD1 cytoplasmic tail sequences could optimally target antigens to the MHC class II antigen presentation pathway. Evaluation of trafficking patterns revealed that all four human CD1-derived targeting sequences delivered antigen to the MHC...
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PMID: 17635609
PDF is available here.
PDF is available here.
Abstract
Three polymorphisms (BamHI, BstNI and HgaI) were identified for inter-species differentiation among standard strains; of which, only HgaI was found to be useful in clinical isolates. Of the 45 isolates, 25 were M. avium and 20 were M. intracelluare. MAC isolates, which could not be differentiated by...
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PMID: 18219086
PDF is available here.
PDF is available here.
Abstract
Chaperonin GroEL assists protein folding in the presence of ATP and magnesium. Recent studies have shown that several divalent cations other than magnesium induce conformational changes of GroEL, thereby influencing chaperonin-assisted protein folding, but little is known about the detailed mechanis...
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PMID: 17242865
PDF is available here.
PDF is available here.
Molecular Pharmacology (72)5 2007
Abstract
Despite the emerging importance of human P450 2B6 in xenobiotic metabolism, thorough biochemical and biophysical characterization has been impeded as a result of low expression in Escherichia coli. Comparison with similar N-terminal truncated and C-terminal His-tagged constructs (rat P450 2B1dH, rab...
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PMID: 17715394
PDF is available here.
PDF is available here.
FASEB Journal (21)11 2007
Abstract
We have reported the mechanism of GroEL/GroES-assisted in vivo and in vitro folding of a 69 kDa monomeric E. coli protein maltodextrin glucosidase (MalZ). Coexpression of GroEL and GroES in E. coli causes a 2-fold enhancement of exogenous MalZ activity in vivo. In vitro, GroEL and GroES in the prese...
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PMID: 17494995
PDF is available here.
PDF is available here.
Microbiology (153)Pt 8 2007
Abstract
I chaperonin GroEL/ES were obtained through inverse PCR, Southern hybridization and sequencing. The G+C ratio of clpB is 49.6 mol%. The predicted ClpB polypeptide contains 869 aa and possesses a long central domain and a predicted distinctly discontinuous coiled-coil motif separating two nucleotide-...
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PMID: 17660421
PDF is available here.
PDF is available here.
Abstract
Chemical synthesis of long or aggregation-prone peptide has been problematic. Its biological production has an advantage in that point, but it often forms inclusion body which creates difficulties in recovery of targets. As a deubiquitylating enzyme (Usp2-cc) was shown in this study to maintain its...
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PMID: 17560941
PDF is available here.
PDF is available here.
Biochemical Journal (404)3 2007
Abstract
We seek to identify and overcome the chemical and biological constraints that limit the evolutionary potential of Rubisco in Nature. Recently, the horizontal transfer of Calvin cycle genes (rbcL, rbcS and prkA) from cyanobacteria (Synechococcus PCC6301) to gamma-proteobacteria (Escherichia coli) was...
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PMID: 17391103
PDF is available here.
PDF is available here.
FEMS Microbiology Letters (271)1 2007
Abstract
Bifidobacteria are natural inhabitants of the human gastrointestinal tract and have been widely used as functional foods in different products. During industrial processing, bacterial cells undergo several stresses that can limit large-scale production and stability of the final product. To better u...
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PMID: 17419761
PDF is available here.
PDF is available here.
Proteomics (7)9 2007
Abstract
We present a robust approach, 2-DE and MALDI-TOF MS, to compare and identify the bacterial proteins responding to the temperature stress. In total, 164 spots of 2-DE were found with the significant changes in spot volume at three culture temperatures, 55, 75, and 80 degrees C, respectively; furtherm...
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PMID: 17469076
PDF is available here.
PDF is available here.
Journal of Molecular Biology (367)4 2007
Abstract
These results showed that at low protein concentrations (<1 mg ml(-1)), the covalent linking of subunits contributes to the stability but also complicates the refolding kinetics. At physiological concentrations of GroES, however, the oligomeric state is energetically preferred and the advantages of...
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PMID: 17303164
PDF is available here.
PDF is available here.
Journal of Molecular Biology (367)3 2007
Abstract
We screened a collection of E. coli mutant strains for their ability to transport a green fluorescent protein (GFP) reporter through the Tat pathway. We found that the molecular chaperone DnaK was essential for cytoplasmic stability of GFP bearing an N-terminal Tat signal peptide, as well as for num...
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PMID: 17280684
PDF is available here.
PDF is available here.
Abstract
We have monitored topology employing disulfide bond formation of a secretory protein, trypsinogen (TG), that behaves in vitro as a stringent, GroEL-GroES-requiring substrate. Inside the long-lived cis chamber formed by SR1, a single-ring version of GroEL, complexed with GroES, we observed an ordered...
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PMID: 17283341
PDF is available here.
PDF is available here.
Abstract
We mutated amino acids in the "mobile loop" regions of N-cpn20, C-cpn20 or both: a highly conserved glycine, which was shown to be important for flexibility of the mobile loop, and a leucine residue shown to be involved in binding of co-chaperonin to chaperonin. The mutant proteins were purified and...
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PMID: 17178727
PDF is available here.
PDF is available here.
Current Microbiology (54)2 2007
Abstract
We have recently shown that X. fastidiosa is a peculiar organism having unusually low values of gene codon bias throughout its genome and, unexpectedly, in the group of the most abundant proteins. Here, we hypothesized that the lack of codon usage optimization in X. fastidiosa would incapacitate thi...
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PMID: 17211542
PDF is available here.
PDF is available here.
Journal of Biotechnology (127)2 2007
Abstract
During production in recombinant Escherichia coli, the human basic fibroblast growth factor (hFGF-2) partly aggregates into stable cytoplasmic inclusion bodies. These inclusion bodies additionally contain significant amounts of the heat-shock chaperone DnaK, and putative DnaK substrates such as the...
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PMID: 16945443
PDF is available here.
PDF is available here.
Abstract
We discuss here a number of issues under current study. What is the range of substrates acted on by the two classes of chaperonin, in particular by GroEL in the bacterial cytoplasm and CCT in the eukaryotic cytosol, and are all these substrates subject to encapsulation? What are the determinants for...
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PMID: 17489689
PDF is available here.
PDF is available here.
Abstract
We introduced a more efficient system to improve and facilitate the soluble production of TEV protease in E. coli. Optimal expression of soluble His6-TEV was achieved by examining the contribution of chaperone co-expression and lower temperature fermentation. When further purified by Ni(2+) affinity...
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PMID: 16919473
PDF is available here.
PDF is available here.
Abstract
Heat and ethanol had an affect not only on growth and cell viability of an obligatorily fermentative Gram-negative bacterium Zymomonas mobilis, but also on protein synthesis. Analysis by SDS-polyacrylamide gel electrophoresis revealed pronounced increasing of two dominant proteins designated as groE...
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PMID: 19069981
PDF is available here.
PDF is available here.
Abstract
We present a novel approach to address this problem. We rely on the premise that, all the residues of the protein machinery (network) must communicate with each other and operate in a coordinated manner to perform their function successfully. To gain insight into the mechanism of information transfe...
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PMID: 17691893
PDF is available here.
PDF is available here.
Abstract
We propose that the duplicate groEL genes in different bacterial clades have evolved independently to meet specific requirements of each clade. We also propose that the groEL gene, although essential and conserved, accumulates nonconservative substitutions to exhibit structural and functional variat...
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PMID: 17103057
PDF is available here.
PDF is available here.
Abstract
Electron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of GroEL (SR398) bound to GroES in the presence of Mg-ATP. This conformation exhibits a considerable expansion of the folding cavity, with approximately 80% more volume than the X-ray structure of the equivalent...
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PMID: 17098196
PDF is available here.
PDF is available here.
Abstract
We modified and optimized a first generation quadrupole time-of-flight (Q-TOF) 1 to perform tandem mass spectrometry on macromolecular protein complexes. The modified instrument allows isolation and subsequent dissociation of high-mass protein complexes through collisions with argon molecules. The m...
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PMID: 17073415
PDF is available here.
PDF is available here.