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Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins

Identifieur interne : 002542 ( Istex/Curation ); précédent : 002541; suivant : 002543

Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins

Auteurs : Timothy Hoey [États-Unis] ; Ya-Lin Sun [États-Unis] ; Keith Williamson [États-Unis] ; Xiang Xu [États-Unis]

Source :

RBID : ISTEX:222E2ED855D00B86AA26031109E1D2A4B401CB97

English descriptors

Abstract

Abstract: The activation of cytoldne genes in response to antigenic stimulation of T cells is mediated by NF-AT proteins. Previous studies have identified two NF-AT proteins, NF-ATp and NF-ATc, that are homologous within a 290 as domain distantly related to the Rel domain. We have isolated two additional members of this gene family, NF-AT3 and NF-AT4, which encode proteins 65% identical to the other NF-AT proteins within the Rel domain. The four NF-AT genes are transcribed in different sets of tissues that Included many sites of expression outside the immune system. The Rel homology domain is sufficient for DNA recognition and cooperative binding Interactions with AP-1. Although other members of the Rel family bind DNA as dimers, NF-AT proteins are monomers in solution or bound to DNA. Transfection assays indicate that each of the four NF-AT proteins can activate the IL-2 promoter in T cells.

Url:
DOI: 10.1016/1074-7613(95)90027-6

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ISTEX:222E2ED855D00B86AA26031109E1D2A4B401CB97

Le document en format XML

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<term>Activation</term>
<term>Affinity chromatography</term>
<term>Amino</term>
<term>Amino acid sequence</term>
<term>Amino acid sequences</term>
<term>Amino acids</term>
<term>Amino sequence</term>
<term>Antigen response element</term>
<term>Antigenic stimulation</term>
<term>Assay</term>
<term>Binding activities</term>
<term>Binding activity</term>
<term>Binding proteins</term>
<term>Binding reactions</term>
<term>Binding site</term>
<term>Binding sites</term>
<term>Biol</term>
<term>Calcium ionophore</term>
<term>Calcium ionophore requirement</term>
<term>Carbonic anhydrase</term>
<term>Cdna</term>
<term>Cdna clones</term>
<term>Cdna fragment</term>
<term>Cell activation</term>
<term>Cjun</term>
<term>Clone</term>
<term>Coding regions</term>
<term>Coli</term>
<term>Composite element</term>
<term>Crabtree</term>
<term>Cyclosporin</term>
<term>Cytokine</term>
<term>Cytokine gene expression</term>
<term>Cytokine genes</term>
<term>Different proteins</term>
<term>Different types</term>
<term>Differential activity</term>
<term>Dimer</term>
<term>Distinct genes</term>
<term>Domain</term>
<term>Elution volumes</term>
<term>Endogenous proteins</term>
<term>Equal amounts</term>
<term>Expression vector</term>
<term>Family members</term>
<term>Filtration</term>
<term>Filtration column</term>
<term>Functional binding sites</term>
<term>Further stimulation</term>
<term>Gene</term>
<term>Gene expression</term>
<term>Gene family</term>
<term>Glycerol</term>
<term>Glycerol gradient</term>
<term>Glycerol gradient centrifugation</term>
<term>Hepg2 cells</term>
<term>Hepgp cells</term>
<term>Homology</term>
<term>Homology domain</term>
<term>Homology region</term>
<term>Human tissues</term>
<term>Immune</term>
<term>Immune response</term>
<term>Immune system</term>
<term>Ionomycin</term>
<term>Ionophore</term>
<term>Jain</term>
<term>Jurkat</term>
<term>Jurkat cells</term>
<term>Lymphocyte</term>
<term>Major sites</term>
<term>Many genes</term>
<term>Mccaffrey</term>
<term>Molecular mass standards</term>
<term>Monomer</term>
<term>Nfat</term>
<term>Nfat genes</term>
<term>Nfat proteins</term>
<term>Nfatp</term>
<term>Nonimmune cells</term>
<term>Northern blot analysis</term>
<term>Northern blots</term>
<term>Northrop</term>
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<term>Nuclear localization</term>
<term>Other proteins</term>
<term>Pbls</term>
<term>Polymerase expression vector</term>
<term>Promoter</term>
<term>Protein</term>
<term>Protein kinase</term>
<term>Proteins bind</term>
<term>Receptor</term>
<term>Reporter gene</term>
<term>Room temperature</term>
<term>Same amounts</term>
<term>Same conditions</term>
<term>Sedimentation positions</term>
<term>Sequence identity</term>
<term>Sequence similarity</term>
<term>Similar affinity</term>
<term>Similarity region</term>
<term>Similarity regions</term>
<term>Skeletal muscle</term>
<term>Skeletal muscle cdna library</term>
<term>Soluble fraction</term>
<term>Stokes</term>
<term>Stokes radii</term>
<term>Stokes radius</term>
<term>Strong expression</term>
<term>Tion</term>
<term>Transcription</term>
<term>Transcription activity</term>
<term>Transcription factor</term>
<term>Transcription factors</term>
<term>Transcriptional</term>
<term>Transcriptional activation</term>
<term>Transcriptional activity</term>
<term>Transfected</term>
<term>Transfection</term>
<term>Transgenic mice</term>
<term>Unpublished data</term>
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<div type="abstract" xml:lang="en">Abstract: The activation of cytoldne genes in response to antigenic stimulation of T cells is mediated by NF-AT proteins. Previous studies have identified two NF-AT proteins, NF-ATp and NF-ATc, that are homologous within a 290 as domain distantly related to the Rel domain. We have isolated two additional members of this gene family, NF-AT3 and NF-AT4, which encode proteins 65% identical to the other NF-AT proteins within the Rel domain. The four NF-AT genes are transcribed in different sets of tissues that Included many sites of expression outside the immune system. The Rel homology domain is sufficient for DNA recognition and cooperative binding Interactions with AP-1. Although other members of the Rel family bind DNA as dimers, NF-AT proteins are monomers in solution or bound to DNA. Transfection assays indicate that each of the four NF-AT proteins can activate the IL-2 promoter in T cells.</div>
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