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  1. Article: The anti-Sm immune response in autoimmunity and cell biology.

    Zieve, Gary W / Khusial, Permanan R

    Autoimmunity reviews

    2003  Volume 2, Issue 5, Page(s) 235–240

    Abstract: Anti-Sm antibodies are found in greater than 30% of the patients with systemic lupus erythematosus (SLE) and are diagnostic of SLE. The Sm autoantigens are the small nuclear ribonucleoprotein (snRNP) common core proteins. The seven core proteins, B, D1, ... ...

    Abstract Anti-Sm antibodies are found in greater than 30% of the patients with systemic lupus erythematosus (SLE) and are diagnostic of SLE. The Sm autoantigens are the small nuclear ribonucleoprotein (snRNP) common core proteins. The seven core proteins, B, D1, D2, D3, E, F and G, shared by a majority of the snRNP particles, form a heptamer ring approximately 20 nm in diameter, with the snRNA passing through the center. The Sm epitopes are distributed on the outside surface of the ring. A repeated proline rich motif with homology to an Epstein bar nuclear antigen in the B protein and a gly-arg-gly motif including a symmetrical dimethylarginine post translational modification in the B, D1 and D3 proteins are major Sm epitopes. The anti-Sm response has features typical of an antigen driven immune response. SnRNP proteins share several characteristics with other autoantigens including their assembly into ribonucleoprotein particles, homologies to known viral proteins, presence of post translational modifications, a high abundance and great stability and the presence of repeated motifs. Current work on the snRNP particles is attempting to identify the features that predispose the common core proteins to become autoantigens in vulnerable individuals.
    MeSH term(s) Animals ; Autoantibodies ; Autoantigens ; Autoimmunity ; Humans ; Lupus Erythematosus, Systemic/etiology ; Lupus Erythematosus, Systemic/immunology ; Ribonucleoproteins, Small Nuclear/chemistry ; Ribonucleoproteins, Small Nuclear/immunology ; snRNP Core Proteins
    Chemical Substances Autoantibodies ; Autoantigens ; Ribonucleoproteins, Small Nuclear ; snRNP Core Proteins
    Language English
    Publishing date 2003-10-03
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2144145-5
    ISSN 1568-9972
    ISSN 1568-9972
    DOI 10.1016/s1568-9972(03)00018-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5913: Show issues Location:
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  2. Article: LSm proteins form heptameric rings that bind to RNA via repeating motifs.

    Khusial, Permanan / Plaag, Robert / Zieve, Gary W

    Trends in biochemical sciences

    2005  Volume 30, Issue 9, Page(s) 522–528

    Abstract: Members of the LSm family of proteins share the Sm fold--a closed barrel comprising five anti-parallel beta strands with an alpha helix stacked on the top. The fold forms a subunit of hexameric or heptameric rings of approximately 7nm in diameter. ... ...

    Abstract Members of the LSm family of proteins share the Sm fold--a closed barrel comprising five anti-parallel beta strands with an alpha helix stacked on the top. The fold forms a subunit of hexameric or heptameric rings of approximately 7nm in diameter. Interactions between neighboring subunits center on an anti-parallel interaction of the fourth and fifth beta strands. In the lumen of the ring, the subunits have the same spacing as nucleotides in RNA, enabling the rings to bind to single-stranded RNA via a repeating motif. Eubacteria and archaea build homohexamers and homoheptamers, respectively, whereas eukaryotes use >18 LSm paralogs to build at least six different heteroheptameric rings. The four different rings in the nucleus that permanently bind small nuclear RNAs and function in pre-mRNA maturation are called Sm rings. The two different rings that transiently bind to RNAs and, thereby, assist in the degradation of mRNA in the cytoplasm and the maturation of a wide spectrum of RNAs in the nucleus are called LSm rings.
    MeSH term(s) Amino Acid Sequence ; Animals ; Archaea/genetics ; Archaea/physiology ; Autoantigens ; Autoimmune Diseases/genetics ; Autoimmune Diseases/physiopathology ; Cytoplasm ; Eukaryotic Cells/physiology ; Humans ; Membranes/chemistry ; Membranes/metabolism ; Membranes/physiology ; Molecular Sequence Data ; Phylogeny ; RNA, Messenger/metabolism ; RNA-Binding Proteins/physiology ; Ribonucleoproteins, Small Nuclear/physiology ; Structure-Activity Relationship ; snRNP Core Proteins
    Chemical Substances Autoantigens ; RNA, Messenger ; RNA-Binding Proteins ; Ribonucleoproteins, Small Nuclear ; snRNP Core Proteins
    Language English
    Publishing date 2005-09
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2005.07.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1207: Show issues Location:
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  3. Article: The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport.

    Khusial, Permanan R / Vaidya, Keta / Zieve, Gary W

    Biochemical and biophysical research communications

    2005  Volume 337, Issue 4, Page(s) 1119–1124

    Abstract: The SmB, SmD1, and SmD3 proteins have the rare symmetrical dimethylarginine post-translational modification in their C-termini. In this report, we investigate the function of this modification in the assembly and intracellular transport of the SmD3 ... ...

    Abstract The SmB, SmD1, and SmD3 proteins have the rare symmetrical dimethylarginine post-translational modification in their C-termini. In this report, we investigate the function of this modification in the assembly and intracellular transport of the SmD3 protein. We show that the elimination of this methylation in the SmD3 protein, by mutating the modified arginines to leucines, does not interfere with the assembly and the nuclear transport of the transiently expressed SmD3 variant. This suggests this modification is not essential for maturation of the SmD3 protein.
    MeSH term(s) Active Transport, Cell Nucleus ; Amino Acid Sequence ; Arginine/analogs & derivatives ; Arginine/metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Humans ; Methylation ; Molecular Sequence Data ; Protein Binding ; Protein Processing, Post-Translational ; Ribonucleoproteins, Small Nuclear/chemistry ; Ribonucleoproteins, Small Nuclear/genetics ; Ribonucleoproteins, Small Nuclear/metabolism
    Chemical Substances Ribonucleoproteins, Small Nuclear ; dimethylarginine ; Arginine (94ZLA3W45F)
    Language English
    Publishing date 2005-12-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2005.09.161
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 116: Show issues Location:
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  4. Article: Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus.

    Miranda, Tina Branscombe / Khusial, Permanan / Cook, Jeffry R / Lee, Jin-Hyung / Gunderson, Samuel I / Pestka, Sidney / Zieve, Gary W / Clarke, Steven

    Biochemical and biophysical research communications

    2004  Volume 323, Issue 2, Page(s) 382–387

    Abstract: We report a novel modification of spliceosome proteins Sm D1, Sm D3, and Sm B/B'. L292 mouse fibroblasts were labeled in vivo with [3H]methionine. Sm D1, Sm D3, and Sm B/B' were purified from either nuclear extracts, cytosolic extracts or a cytosolic 6S ... ...

    Abstract We report a novel modification of spliceosome proteins Sm D1, Sm D3, and Sm B/B'. L292 mouse fibroblasts were labeled in vivo with [3H]methionine. Sm D1, Sm D3, and Sm B/B' were purified from either nuclear extracts, cytosolic extracts or a cytosolic 6S complex by immunoprecipitation of the Sm protein-containing complexes and then separation by electrophoresis on a polyacrylamide gel containing urea. The isolated Sm D1, Sm D3 or Sm B/B' proteins were hydrolyzed to amino acids and the products were analyzed by high-resolution cation exchange chromatography. Sm D1, Sm D3, and Sm B/B' isolated from nuclear fractions were all found to contain omega-NG-monomethylarginine and symmetric omega-NG,NG'-dimethylarginine, modifications that have been previously described. In addition, Sm D1, Sm D3, and Sm B/B' were also found to contain asymmetric omega-NG,NG-dimethylarginine in these nuclear fractions. Analysis of Sm B/B' from cytosolic fractions and Sm B/B' and Sm D1 from cytosolic 6S complexes showed only the presence of omega-NG-monomethylarginine and symmetric omega-NG,NG'-dimethylarginine. These results indicate that Sm D1, Sm D3, and Sm B/B' are asymmetrically dimethylated and that these modified proteins are located in the nucleus. In reactions in which Sm D1 or Sm D3 was methylated in vitro with a hemagglutinin-tagged PRMT5 purified from HeLa cells, we detected both symmetric omega-NG,NG'-dimethylarginine and asymmetric omega-NG,NG-dimethylarginine when reactions were done in a Tris/HCl buffer, but only detected symmetric omega-NG,NG'-dimethylarginine when a sodium phosphate buffer was used. These results suggest that the activity responsible for the formation of asymmetric dimethylated arginine residues in Sm proteins is either PRMT5 or a protein associated with it in the immunoprecipitated complex.
    MeSH term(s) Amino Acid Sequence ; Animals ; Arginine/chemistry ; Arginine/metabolism ; Binding Sites ; Cell Extracts/chemistry ; Cell Line ; Cell Nucleus/chemistry ; Cell Nucleus/metabolism ; Fibroblasts/metabolism ; Fibroblasts/ultrastructure ; HeLa Cells ; Humans ; Methylation ; Mice ; Molecular Sequence Data ; Protein Binding ; Ribonucleoproteins, Small Nuclear/chemistry ; Ribonucleoproteins, Small Nuclear/metabolism ; Spliceosomes/chemistry ; Spliceosomes/metabolism ; Structure-Activity Relationship
    Chemical Substances Cell Extracts ; Ribonucleoproteins, Small Nuclear ; Arginine (94ZLA3W45F)
    Language English
    Publishing date 2004-10-15
    Publishing country United States
    Document type Comparative Study ; Evaluation Studies ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2004.08.107
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
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