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Topic: GroEL

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Chaperone

Heat shock protein

Hsp70

	Analysis of GroEL substrates
		The hydrophobic binding regions of GroEL may be well adapted to interact with the non-native states of alpha/beta-domain proteins.
		The positions of 52 identified GroEL substrates on the coomassie-stained 2D gel are indicated.
		The differences observed (asterisk) between the E. coli set and the GroEL substrates were found to be statistically significant at the 95% confidence limit by using equations developed for sampling statistics.
	pedant.gsf.de /GROEL/index.html (335 words)

	Protein Science 5(3):478-487. GroEL-beta-galactosidase interaction (Site not responding. Last check: 2007-10-19)
		The positive effect of GroEL alone on the refolding of beta-galactosidase was quite unexpected because the formation of stable binary complexes between the chaperonin and its substrates typically arrests refolding (Hartl et al., 1994).
		Presumably, ATP binding and hydrolysis lowers the affinity of GroEL for beta-galactosidase, causing the discharge of an aggregation-prone folding intermediate from the chaperonin and/or preventing its rebinding.
		GroEL was purified from clarified cell extracts according to protocols published previously (Goloubinoff et al., 1989a).
	faculty.washington.edu /baneyx/pub/PS96.html (7082 words)

	Palaeos Bacteria: Pieces: GroEL
		The key to the activity of GroEL is in the structure of the monomer, shown in the next image from Ranson et al.
		GroEL is a complicated molecule and, doubtless, there are any number of ways in which a polypeptide can interact with it.
		Like the kitchen spoon, GroEL is a device which is both ubiquitous and unspecialized -- not part of the recipie, but one of the basic tools around which the whole idea of a recipie is built.
	www.palaeos.com /Bacteria/Pieces/GroEL.html (1616 words)

	GroEL - Wikipedia, the free encyclopedia
		GroEL is a protein chaperone required for the proper folding of many proteins in prokaryotes, chloroplasts, and mitochondria.
		(GroEL and GroES are also sometimes referred to as chaperonin and cochaperonin, or chaperonin 60 and chaperonin 10 for their molecular weights.) In eukaryotes the proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively.
		GroEL is a very complicated molecule and, doubtless, there are any number of ways in which a polypeptide can interact with it.
	en.wikipedia.org /wiki/GroEL (1715 words)

	UCSF Chimera - GroEL Visualization
		GroEL is a cylindrical 14-mer that refolds misfolded proteins in its interior cavity.
		To clip the GroEL density perpendicular to the cylindrical axis, first press the Orient button on at the bottom of the Volume Viewer dialog, then press the Orient plane perpendicular to line of sight button on the Per-Model Clipping dialog.
		GroEL adopts different conformations and our hand alignment of PDB model 1OEL and density map emd_1080 is only a first step in comparing this crystal and single particle EM data.
	www.cgl.ucsf.edu /chimera/tutorials/groel/groel.html (3739 words)

	Potato Leafroll Virus Binds to the Equatorial Domain of the Aphid Endosymbiotic GroEL Homolog -- Hogenhout et al. 72 ... (Site not responding. Last check: 2007-10-19)
		GroEL was isolated from the endosymbiotic bacteria of 6-day-old M.
		A radiolabeled PCR fragment comprising the gene encoding MpB GroEL was used as the probe.
		The positions of GroEL (60 kDa), GST (28 kDa), and the smallest truncated MpB GroEL fragments that bind PLRV [(409-548) and (1-121)] are indicated by arrowheads.
	jvi.asm.org /cgi/content/full/72/1/358 (5150 words)

	In vivo activities of GroEL minichaperones -- Chatellier et al. 95 (17): 9861 -- Proceedings of the National Academy of ...
		In vitro refolding of rhodanese in the presence of GroEL minichaperones.
		coli SV2 (groEL44) and SV6 (groEL673) strains by overexpression of GroEL or minichaperones.
		GroEL is involved in activation of Escherichia coli RNA polymerase devoid of the {omega} subunit in vivo
	www.pnas.org /cgi/content/full/95/17/9861 (3792 words)

	GroEL of Lactobacillus johnsonii La1 (NCC 533) Is Cell Surface Associated: Potential Role in Interactions with the Host ...
		GroEL of Lactobacillus johnsonii La1 (NCC 533) Is Cell Surface Associated: Potential Role in Interactions with the Host and the Gastric Pathogen Helicobacter pylori -- Bergonzelli et al.
		The presence of GroEL at the surface of La1 was determined by ELISA as described in Materials and Methods using a polyclonal anti-GroEL antibody as the primary antibody (•).
		GroEL heat shock protein of Haemophilus ducreyi: association with cell surface and capacity to bind to eukaryotic cells.
	iai.asm.org /cgi/content/full/74/1/425 (5495 words)

	BioMed Central \| Full text \| Differential gene transfers and gene duplications in primary and secondary endosymbioses
		The secondary endosymbionts of a cryptomonad (Guillardia theta) and also a diatom (Odontella sinensis) are known to encode a single groEL gene in their plastid, and it can be speculated that the presence of a single copy of groEL may indicate the ancestral state in a primary endosymbiont [8,9].
		In the earliest cyanobacterial-like prokaryotes, the ancestral groEL sequence appears to have duplicated to form an "A" and a "B" type sequence that is still present today in the genome of Gloeobacter [14,15].
		PCC 6803, we have adopted the terminology of "groEL1" and "groEL 2".
	www.biomedcentral.com /1471-2148/6/38 (3225 words)

	Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding ...
		The sample of GroEL (80 µg of immobilized protein) was incubated for 30 min with 1.9 µM Y283V dimers and washed with a 30-fold volume of the refolding buffer (lane 1) or the buffer containing 3 mM Mg-ATP (lane 2).
		by immunization of rabbits with the wild-type GroEL or GAPDH
		GroEL was purified as described by Corrales and Fersht (1996).
	www.proteinscience.org /cgi/content/full/14/4/921 (4566 words)

	GroES Mobile Loop
		Escherichia coli GroEL and GroES are the prototypical chaperonin and co-chaperonin.
		GroEL is composed of fourteen identical 60 kDa subunits arranged in two stacked rings, and GroES is composed of a seven identical 10 kDa subunits.
		Thus, the structure was determined by analysis of transferred nuclear Overhauser effects (trNOEs) in NMR spectra of the peptide in the presence of GroEL.
	www.tulane.edu /~biochem/sam/billboard.htm (1350 words)

	Atomic Force Microscopy Detects Changes in the Interaction Forces between GroEL and Substrate Proteins -- Vinckier et ...
		the chaperonin GroEL and its cochaperonin GroES (Hartl, 1996
		GroEL (1.4 µM) in MOPS buffer was allowed to adsorb on freshly cleaved mica (Goodfellow, Cambridge, England).
		GroEL are 13.7 nm for the diameter, 14.6 nm for the height, and
	www.biophysj.org /cgi/content/full/74/6/3256 (4361 words)

	GroEL (Hsp60) of Clostridium difficile is involved in cell adherence -- Hennequin et al. 147 (1): 87 -- Microbiology
		GroEL (Hsp60) of Clostridium difficile is involved in cell adherence -- Hennequin et al.
		fragment of the groELS operon of strains 79-685 and ATCC 53603
		GroEL was detected by immunoblotting (1:2000 dilution of antibodies).
	mic.sgmjournals.org /cgi/content/full/147/1/87 (5363 words)

	Characterization of the groEL and groES Loci in Bifidobacterium breve UCC 2003: Genetic, Transcriptional, and ...
		Characterization of the groEL and groES Loci in Bifidobacterium breve UCC 2003: Genetic, Transcriptional, and Phylogenetic Analyses -- Ventura et al.
		Characterization of the groEL and groES Loci in Bifidobacterium breve UCC 2003: Genetic, Transcriptional, and Phylogenetic Analyses
		The estimated length of the transcript corresponding to the hybridization signal is indicated.
	aem.asm.org /cgi/content/full/70/10/6197 (6517 words)

	Apple - Science - Inside the Image - Modeling GroEL
		First, GroEL protein was isolated and crystallized, and an atomic model of the protein created.
		Since the GroEL complex shown in the image contains 14 copies of the monomeric crystal structure, the resulting detailed three-dimensional atomic model was then docked into the an electron microscope density map in order to create the overall model of the biologically active protein complex.
		Molecular complexes are of keen scientific interest in biology today, and hence the ability to visualize these complex entities is critical our understanding of their structure and function.
	www.apple.com /science/insidetheimage/groel (1369 words)

	Molecular Analysis of the Multiple GroEL Proteins of Chlamydiae -- Karunakaran et al. 185 (6): 1958 -- The Journal of ...
		GroELs are implicated in bacterial disease pathogenesis (41),
		GroEL2 and GroEL3 cluster in an offshoot from GroELs of the
		The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.
	jb.asm.org /cgi/content/full/185/6/1958 (4188 words)

	Porous rollers offer new approach to tape path design challenges--Peter Groel Mountain Engineering II in Data Storage ...
		Another advantage of the porous roller is that a tachometer can be attached to it, and since the spool spins at the same rate as the tape movement, it is possible to accurately and consistently measure tape speed by measuring spool speed.
		Peter Groel is president of Mountain Engineering II in Longmont, Colorado.
		Groel can be contacted through the company website at www.mountainengineering.com, by phone at 303-651-0277 ext 11, or via email at peterg@mountainengineering.com.
	www.mountainengineering.com /dsm/DSMarticle.html (1862 words)

	Molecular cloning of the Chlamydophila abortus groEL gene and evaluation of its protective efficacy in a murine model ...
		Molecular cloning of the Chlamydophila abortus groEL gene and evaluation of its protective efficacy in a murine model by genetic vaccination -- Héchard et al.
		GroEL was measured using the BCA protein assay reagent (Pierce)
		GroEL was detected after Western blotting with the anti-GroEL mAb A57-B9.
	jmm.sgmjournals.org /cgi/content/full/53/9/861 (4651 words)

	FtsZ-dependent localization of GroEL protein at possible division sites -- Ogino et al. 9 (9): 765 -- Genes to Cells
		GroEL protein is originally localized at the centre of cells.
		Shinnick, T.M., Vodkin, M.H. and Williams, J.C. (1988) The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein.
		Viitanen, P.V., Gatenby, A.A. and Lorimer, G.H. (1992) Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins.
	www.genestocellsonline.org /cgi/content/full/9/9/765 (2824 words)

	GroEL/GroES (Site not responding. Last check: 2007-10-19)
		GroEL and GroES work together (interact) to help peoteins fold into their native state properly.
		GroEL is made up of two sets of rings (blue/cyan and green/yellow).
		GroEL, on the other hand, stretches and twists.
	www.cra.org /Activities/craw/dmp/awards/miller/groel-es.html (191 words)

	JSWlab :: Research
		Chaperonins, such as E. coli GroEL, are large ring structures that aid folding a wide variety of proteins in the cytosol of all organisms.
		The long-term goal of our chaperonin studies is to understand the physical basis by which chaperonins assist folding as well as how the particular “cocktail” of chaperones present in a given cell helps determine the spectrum of proteins that can fold.
		To understand the basis and extent of the chaperonin substrate spectrum, we used rounds of selection and DNA shuffling to obtain GroEL/S variants that dramatically enhanced folding of a single substrate–green fluorescent protein (GFP).
	www.ucsf.edu /jswlab/research_chap.html (241 words)

	groEL Encodes a Highly Antigenic Protein in Burkholderia pseudomallei -- Woo et al. 8 (4): 832 -- Clinical and Vaccine ...
		Phylogenetic trees based on known bacterial GroEL amino acid sequences (a), nucleotide sequences (b), and their corresponding 16S rRNA gene sequences (c) illustrating the position of B.
		on the nucleotide sequences of the groEL genes of the bacteria
		The nucleotide sequence of the groEL gene of B.
	cdli.asm.org /cgi/content/full/8/4/832 (2600 words)

	PCR Assay of the groEL Gene for Detection and Differentiation of Bacillus cereus Group Cells -- Chang et al. 69 (8): ...
		A phylogenetic analysis of the groEL sequences of 78 B.
		PCR amplification of groEL gene and sodA gene.
		An internal portion of the groEL gene was amplified by PCR with
	aem.asm.org /cgi/content/full/69/8/4502 (3514 words)

	[No title]
		Partially folded polypeptide chains, either newly made by ribosomes or emerging from mature proteins unfolded by stress, run the risk of aggregating with one another to the detriment of the organism.
		GroEL and GroES prevent aggregation by encapsulating individual chains within the so-called Â‘Anfinsen cageÂ’ provided by the GroELÂ—GroES complex, where they can fold in isolation from one another [1].
		GroEL consists of two heptameric rings of identical ATPase subunits stacked back to back, containing a cage in each ring.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR008950 (402 words)

	Chlamydial GroEL Autoregulates Its Own Expression through Direct Interactions with the HrcA Repressor Protein -- Wilson ...
		P radioactivity signal of samples corresponding to lanes in the Western blot are represented in a bar graph.
		P-labeled DNA probe containing the CIRCE element was incubated with several protein preparations, and the resulting complexes were resolved by native polyacrylamide gel electrophoresis.
		ATP to GroEL did not augment the effect of GroEL on HrcA (Fig.
	jb.asm.org /cgi/content/full/187/21/7535 (5210 words)

	Eliminating Reel Motor Position Sensor in a Tape Drive--Peter Groel Mountain Engineering II in Computer Technology ...
		Eliminating Reel Motor Position Sensor in a Tape Drive--Peter Groel Mountain Engineering II in Computer Technology Review-Dec. 2001 & Jan. 2002 issues
		Peter Groel is president of Mountain Engineering II, Inc. in Longmont, Colorado.
		Groel can be contacted at MEII by phone 303-651-0277 ext.
	www.mountainengineering.com /CRT/article1.html (2450 words)

	Subcellular Localization and Cytotoxic Activity of the GroEL-Like Protein Isolated from Actinobacillus ...
		The potent bone-resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL.
		SMITHERMAN, L. Bartonella bacilliformis GroEL: Effect on Growth of Human Vascular Endothelial Cells in Infected Cocultures.
		Hennequin, C., Porcheray, F., Waligora-Dupriet, A.-J., Collignon, A., Barc, M.-C., Bourlioux, P., Karjalainen, T. GroEL (Hsp60) of Clostridium difficile is involved in cell adherence.
	iai.asm.org /cgi/content/full/66/11/5307 (4826 words)

	Python Success Stories
		Since my research work is focused on the development of new simulation techniques, modifiability was a particularly important criterion.
		Dynamic deformation of the chaperon protein GroEL, obtained with the MMTK-based interactive DomainFinder (Zoom in)
		Characteristic features of biomolecular simulations that had to be taken into account are the long execution times of some simulation techniques (several weeks are not uncommon) and the complexity of the data structures describing biomolecules.
	www.python.org /about/success/mmtk (817 words)

	Dr. Carl Frieden's Groel References (Site not responding. Last check: 2007-10-19)
		Clark, A. C., Karon, B. and Frieden, C. (1999) Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL.
		Clark, A.C. & Frieden, C. (1999) The Chaperonin GroEL Binds to Late Folding Non-native Conformations Present in Native E.
		Clark, A. Clay, Eric Hugo, and Carl Frieden (1996) Determination of Regions in the Dihydrofolate Reductase Structure that Interact with the Molecular Chaperonin GroEL.
	www.biochem.wustl.edu /cflab/groelref.html (205 words)

	The Chaperonin Home Page (Site not responding. Last check: 2007-10-19)
		This page will provide vital information to all researchers in the field of heat shock proteins.
		Includes the GroEL PDB files and a kinemage tour of the GroES structure
		The crystal structure of a GroEL 14mer complexed with ATP-gamma-S
	biochem.uthscsa.edu /seale/Chap/chap.html (115 words)

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