29 results match your criteria gamma-b-crystallin

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Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations.

Mol Cell 2016 Feb;61(3):341-351

Center for Gene Regulation in Health and Disease and Department of Biological, Geological and Environmental Sciences, Cleveland State University, Cleveland, Ohio 44115, USA.

In all genomes, most amino acids are encoded by more than one codon. Synonymous codons can modulate protein production and folding, but the mechanism connecting codon usage to protein homeostasis is not known. Here we show that synonymous codon variants in the gene encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotranslational folding of protein domains monitored in real time by Förster resonance energy transfer and fluorescence-intensity changes. Read More

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February 2016

Using SecM arrest sequence as a tool to isolate ribosome bound polypeptides.

J Vis Exp 2012 Jun 19(64). Epub 2012 Jun 19.

Center for Gene Regulation in Health and Disease, Department of Biological, Geological and Environmental Sciences, Cleveland State University, USA.

Extensive research has provided ample evidences suggesting that protein folding in the cell is a co-translational process. However, the exact pathway that polypeptide chain follows during co-translational folding to achieve its functional form is still an enigma. In order to understand this process and to determine the exact conformation of the co-translational folding intermediates, it is essential to develop techniques that allow the isolation of RNCs carrying nascent chains of predetermined sizes to allow their further structural analysis. Read More

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A novel human CRYGD mutation in a juvenile autosomal dominant cataract.

Mol Vis 2010 May 22;16:887-96. Epub 2010 May 22.

Department of Biotechnology, Manipal Life Sciences Centre, Manipal University, Manipal, Karnataka state, India.

Purpose: Identification of causal mutation in the crystallin, connexin, and paired box gene 6 (PAX6) genes associated with childhood cataract in patients from India.

Methods: In this study, forty eight members from seventeen families and 148 sporadic cases of childhood cataract were evaluated. Clinical and ophthalmologic examinations were performed on available affected and unaffected family members. Read More

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Structures of differently aggregated and precipitated forms of gamma B crystallin: an FTIR spectroscopic and EM study.

Protein Pept Lett 2010 Sep;17(9):1155-62

Department of Protein Science & Engineering, Institute of Microbial Technology (IMTECH), Chandigarh 160036, India.

The lens protein, gamma B-crystallin, precipitates during cataract formation. As a recombinant protein, in aqueous solution, gamma B aggregates and precipitates upon heating, cooling, exposure to ultraviolet light, or refolding from a denatured state. We have studied soluble gamma B crystallin, as well as each of the above aggregated forms, to determine whether gamma B's polypeptide chain is differently organized in each form. Read More

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September 2010

Affilin-novel binding molecules based on human gamma-B-crystallin, an all beta-sheet protein.

J Mol Biol 2007 Sep 22;372(1):172-85. Epub 2007 Jun 22.

Scil Proteins GmbH, Heinrich Damerow Str. 1, 06120 Halle (Saale), Germany.

The concept of novel binding proteins as an alternative to antibodies has undergone rapid development and is now ready for practical use in a wide range of applications. Alternative binding proteins, based on suitable scaffolds with desirable properties, are selected from combinatorial libraries in vitro. Here, we describe an approach using a beta-sheet of human gamma-B-crystallin to generate a universal binding site through randomization of eight solvent-exposed amino acid residues selected according to structural and sequence analyses. Read More

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September 2007

Interaction of lens alpha and gamma crystallins during aging of the bovine lens.

Exp Eye Res 2005 Dec 20;81(6):680-9. Epub 2005 Jun 20.

Division of Biology, Ackert Hall, Kansas State University, Manhattan, KS 66506, USA.

Heterologous, noncovalent interactions of lens crystallins, such as between alpha and gamma crystallin, are thought to play a key role in the transparent properties of the lens. To determine possible interactions between these two types of crystallins, bovine gamma B crystallin in its native state was purified from whole fetal lenses or from the nucleus of aged bovine lenses, and the purified protein was passed over immobilized alpha crystallin, using a surface plasmon resonance instrument (BIAcore 3000) to obtain refractive units (RU) of gamma B binding at equilibrium. The results demonstrate low binding of gamma B crystallin purified from fetal lenses, but higher binding of the same gamma species purified from aged lenses. Read More

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December 2005

Prediction of possible sites for posttranslational modifications in human gamma crystallins: effect of glycation on the structure of human gamma-B-crystallin as analyzed by molecular modeling.

Proteins 2003 Nov;53(2):162-73

H.E.J. Research Institute of Chemistry, International Center for Chemical Sciences, University of Karachi, Karachi, Pakistan.

Crystallins are recognized as one of the long-lived proteins of lens tissue that might serve as the target for several posttranslational modifications leading to cataract development. We have studied several such sites present in the human gamma-crystallins based either on PROSITE pattern search results or earlier experimental evidences. Their probabilities were examined on the basis of the database analysis of the gamma-crystallin sequences and on their specific locations in the constructed homology models. Read More

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November 2003

Molecular pathology of dityrosine cross-links in proteins: structural and functional analysis of four proteins.

Mol Cell Biochem 2002 May-Jun;234-235(1-2):27-38

Hyderabad Eye Research Foundation, LV Prasad Eye Institute, India.

The dityrosine bond (DT) is an oxidative covalent cross-link between two tyrosines. DT cross-linking is increasingly identified as a marker of oxidative stress, aging and disease, and has been detected in diverse pathologies. While DT cross- linked proteins have been documented, the consequences of the DT link on the structure and function of the so modified proteins are yet to be understood. Read More

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February 2003

Mouse models of congenital cataract.

J Graw

Eye (Lond) 1999 Jun;13 ( Pt 3b):438-44

GSF-Forschungszentrum für Umwelt und Gesundheit Institut für Säugetiergenetik, Neuherberg Germany.

Mouse mutants affecting lens development are excellent models for corresponding human disorders. The mutant aphakia has been characterised by bilaterally aphakic eyes (Varnum and Stevens, J Hered 1968;59:147-50); the corresponding gene was mapped to chromosome 19 (Varnum and Stevens, Mouse News Lett 1975;53:35). Recent investigations in our laboratory refined the linkage of 0. Read More

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Cataract mutations and lens development.

J Graw

Prog Retin Eye Res 1999 Mar;18(2):235-67

GSF-National Research Center for Environment and Health, Institute of Mammalian Genetics, Neuherberg, Germany.

The lens plays an essential role for proper eye development. Mouse mutants affecting lens development are excellent models for corresponding human disorders. Moreover, using mutations in particular genes the process of eye and lens development can be dissected into distinct steps. Read More

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Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens.

Protein Sci 1997 Jul;6(7):1529-36

Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.

gamma B-crystallin is a monomeric member of the beta gamma-superfamily of vertebrate eye lens proteins. It consists of two similar domains with all-beta Greek key topology associating about an approximate two-fold axis. At pH 2, with urea as the denaturant, the domains show independent equilibrium unfolding transitions, suggesting different intrinsic stabilities. Read More

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Pantethine inhibits the formation of high-Tc protein aggregates in gamma B crystallin solutions.

Curr Eye Res 1996 Dec;15(12):1182-90

Department of Physics, Massachusetts Institute of Technology, Cambridge, USA.

Purpose: Solutions of the bovine lens protein gamma B (or gamma II) crystallin at neutral pH in the absence of reducing agents, undergo a slow, partial conversion to a new protein species, gamma IIH. This species is an aggregate composed of an intermolecular, disulfide-crosslinked dimer (approximately equal to 32% of total protein by weight) and loosely associated dimers (approximately equal to 66%). gamma IIH has a phase separation temperature (Tph), at least 40 degrees C higher than that of native gamma II crystallin at any given protein concentration. Read More

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December 1996

LP2, a differentiation-associated lipid-binding protein expressed in bovine lens.

C Jaworski G Wistow

Biochem J 1996 Nov;320 ( Pt 1):49-54

Section on Molecular Structure and Function, LMDB, National Eye Institute, National Institutes of Health, Bethesda, MD 20892-2730, USA.

A 13 kDa protein from bovine lens was identified and characterized by protein microsequencing and by rapid amplification of cDNA ends (RACE) PCR. Its complete sequence shows that this protein belongs to a family of fatty acid-binding proteins (FABPs), including myelin and adipocyte P2, that are associated with cellular differentiation. The bovine lens protein, designated LP2, shows very close similarity to human epidermal FABP (eFABP) and human eFABP was detected in human lens, suggesting that the two proteins might be orthologous. Read More

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November 1996

Kinetics of translation of gamma B crystallin and its circularly permutated variant in an in vitro cell-free system: possible relations to codon distribution and protein folding.

FEBS Lett 1995 Dec;376(3):195-8

Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.

Analysis of nascent gamma B-crystallin peptides accumulating during in vitro translation in a rabbit reticulocyte lysate cell-free system was carried out. As a consequence of the irregular distribution of rare codons along the polypeptide chain of gamma B-crystallin, translation of the two-domain protein is a non-uniform process characterized by specific pauses. One of the major delays occurs during the translation of the connecting peptide between the domains. Read More

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December 1995

Role of glycine 1 and lysine 2 in the glycation of bovine gamma B-crystallin. Site-directed mutagenesis of lysine to threonine.

J Biol Chem 1995 Sep;270(35):20781-6

Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912-2100, USA.

To determine the role of Gly-1 and Lys-2 of bovine gamma B-crystallin in glycation and cross-linking, Lys-2 was changed to Thr by site-directed mutagenesis. A polymerase chain reaction was used to perform site-directed mutagenesis on the third codon (AAG-->ACG) of bovine gamma B-crystallin cDNA. The wild type and mutant cDNAs were cloned into pMON5743 and expressed in JM101 Escherichia coli cells, and the identity of gamma B-crystallin was confirmed by Western blotting after purification by cation exchange high performance liquid chromatography. Read More

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September 1995

Modelling molecular stability in gamma B crystallin.

D Goode M J Crabbe

Comput Chem 1995 Jun;19(2):65-74

Wolfson Laboratory, School of Animal and Microbial Sciences, University of Reading, White Knights, England.

Molecular modelling and dynamics simulations of gamma B crystallin and a number of its adducts were used to simulate effects of post-translational modifications. N-terminal modifications which disrupted the surface charge network of gamma-crystallin did not produce significant unfolding in any part of the gamma-crystallin molecule (P > 0.05) consistent with the results of in vitro aggregation studies. Read More

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Oxidation of gamma II-crystallin solutions yields dimers with a high phase separation temperature.

Proc Natl Acad Sci U S A 1995 Feb;92(4):1067-71

Department of Physics, Massachusetts Institute of Technology, Cambridge 02139.

Aqueous solutions of the bovine eye lens protein gamma II (or gamma B)-crystallin at neutral pH show a gradual increase in phase separation temperature, Tph, when allowed to stand for several weeks at room temperature without reducing agents. In a typical experiment, the Tph of the protein solution (218 mg/ml) increases from 2.5 +/- 1 degree C to 32. Read More

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February 1995

Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions.

Exp Eye Res 1994 Nov;59(5):607-16

Australian Cataract Research Foundation, Department of Chemistry, University of Wollongong, NSW, Australia.

alpha-, beta- and gamma-crystallins from bovine lens contain flexible terminal extensions which are readily observed by NMR spectroscopy. By monitoring these resonances, NMR spectroscopy therefore offers a means of examining specific protein-protein interactions in crystallin mixtures. In this paper, a 1H NMR spectroscopic study of bovine lens nuclear and cortical homogenates and various crystallin mixtures is presented. Read More

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November 1994

Three-dimensional model and quaternary structure of the human eye lens protein gamma S-crystallin based on beta- and gamma-crystallin X-ray coordinates and ultracentrifugation.

Protein Sci 1994 Oct;3(10):1840-6

H.E.J. Research Institute of Chemistry, University of Karachi, Pakistan.

A 3-dimensional model of the human eye lens protein gamma S-crystallin has been constructed using comparative modeling approaches encoded in the program COMPOSER on the basis of the 3-dimensional structure of gamma-crystallin and beta-crystallin. The model is biased toward the monomeric gamma B-crystallin, which is more similar in sequence. Bovine gamma S-crystallin was shown to be monomeric by analytical ultracentrifugation without any tendency to form assemblies up to concentrations in the millimolar range. Read More

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October 1994

Dimerization of beta B2-crystallin: the role of the linker peptide and the N- and C-terminal extensions.

Protein Sci 1994 Sep;3(9):1392-400

Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.

beta B2- and gamma B-crystallins of vertebrate eye lens are 2-domain proteins in which each domain consists of 2 Greek key motifs connected by a linker peptide. Although the folding topologies of beta B2- and gamma B-domains are very similar, gamma B-crystallin is always monomeric, whereas beta B2-crystallin associates to homodimers. It has been suggested that the linker or the protruding N- and C-terminal arms of beta B2-crystallin (not present in gamma B) are a necessary requirement for this association. Read More

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September 1994

Aggregation of beta A3-crystallin is independent of the specific sequence of the domain connecting peptide.

J Biol Chem 1994 Aug;269(33):21141-5

Laboratory of Mechanisms of Ocular Diseases, National Eye Institute, NICHD, National Institutes of Health, Bethesda, Maryland 20892.

The beta- and gamma-crystallins are structural proteins whose high concentration and close packing are important in maintaining transparency of the eye lens. The beta gamma-crystallin superfamily includes proteins with similar core structures consisting of two compact domains linked by a short connecting peptide. In gamma-crystallins, the connecting peptide folds back on itself, allowing the amino and carboxyl domains to participate in close interactions. Read More

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A 1H NMR spectroscopic comparison of gamma S- and gamma B-crystallins.

Exp Eye Res 1994 Aug;59(2):211-20

Australian Cataract Research Foundation, University of Wollongong, NSW.

Two-dimensional 1H NMR spectroscopic studies are presented on bovine gamma S- and gamma B-crystallin. In gamma S-crystallin, the four N-terminal residues have great flexibility compared with the rest of the molecule and assume a random coil conformation. NMR spectroscopy and electrospray mass spectrometry show that the N-terminal residue is acetylated. Read More

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Alpha-crystallin: molecular chaperone and protein surfactant.

Biochim Biophys Acta 1994 Feb;1204(2):195-206

Australian Cataract Research Foundation, Department of Chemistry, University of Wollongong, NSW.

Bovine lens alpha-crystallin has recently been shown to function as a molecular chaperone by stabilizing proteins against heat denaturation (Horwitz, J. (1992) Proc. Natl. Read More

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February 1994

NMR-derived three-dimensional solution structure of protein S complexed with calcium.

Structure 1994 Feb;2(2):107-22

Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.

Background: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is evolutionarily related to vertebrate lens beta gamma-crystallins. Read More

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February 1994

Domain interactions and connecting peptides in lens crystallins.

J Mol Biol 1994 Jan;235(1):84-8

Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.

beta B2- and gamma B-crystallin from bovine eye-lens are closely related proteins, topologically distinct mainly by virtue of the linker peptide connecting the two domains in each polypeptide chain. In homodimeric beta B2-crystallin, the extended conformation of the connecting peptide has been suggested to force the beta B2-molecule to favor intermolecular domain interactions compared with intramolecular contacts in monomeric gamma B-crystallin. From this one may postulate that the conserved interdomain contacts are essential for the overall stability of crystallins. Read More

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January 1994

High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin.

J Mol Biol 1991 Dec;222(4):1067-83

Laboratory of Molecular Biology, Birkbeck College, London University, U.K.

beta-Crystallins are polydisperse, oligomeric structural proteins that have a major role in forming the high refractive index of the eye lens. Using single crystal X-ray crystallography with molecular replacement, the structure of beta B2 dimer has been solved at 2.1 A resolution. Read More

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December 1991

Trinucleotide repeat polymorphism at the human gamma-B-crystallin gene.

Nucleic Acids Res 1991 Aug;19(16):4571

National Institute of Mental Health Neuroscience Center, St Elizabeths Hospital, Washington, DC 20032.

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The reaction of singlet oxygen with proteins, with special reference to crystallins.

Photochem Photobiol 1990 Oct;52(4):761-8

Laboratory of Mechanisms of Ocular Disease, National Eye Institute, NIH, Bethesda, MD.

Photosensitized oxidation of the eye lens proteins, the crystallins, is thought to lead to protein crosslinks and high molecular weight aggregates. Such protein modifications may be important factors in the formation of lens opacities or cataracts. We focus attention here on type 2 photo-oxidation involving the reaction of singlet oxygen (1O2) with crystallins and some "control" proteins. Read More

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October 1990
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