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Galina G. Karpova - One of the best experts on this subject based on the ideXlab platform.
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binding of the ires of hepatitis c virus rna to the 40s ribosomal subunit role of P40
Molecular Biology, 2009Co-Authors: Alexey A. Malygin, Olga Kossinova, E I Bondarenko, Valery B. Loktev, Z. V. Bochkaeva, Ivan N. Shatsky, Galina G. KarpovaAbstract:Ribosomal Protein P40 is a structural component of the eukaryotic 40S ribosomal subunit, is partly homologous to prokaryotic ribosomal Protein S2, and has a long eukaryote-specific C-terminal region. The internal ribosome entry site (IRES) of the hepatitis C virus (HCV) RNA was tested for the binding to 40S ribosomal subunits deficient in P40, saturated with recombinant P40, or pretreated with monoclonal antibody (MAB) 4F6 against P40. The apparent association constant of HCV IRES binding to 40S subunits was shown to directly depend on the P40 content in the subunits. MAB 4F6 prevented HCV IRES binding to 40S subunits and blocked translation of IRES-containing RNA in a cell-free translation system. The results implicate P40 in the binding of the HCV IRES to the ribosome and, therefore, in translation initiation on HCV RNA.
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Binding of the IRES of hepatitis C virus RNA to the 40S ribosomal subunit: role of Protein P40
Molekuliarnaia biologiia, 2009Co-Authors: Alexey A. Malygin, E I Bondarenko, Valery B. Loktev, Z. V. Bochkaeva, O A Kosinova, I N Shatskiĭ, Galina G. KarpovaAbstract:Ribosomal Protein P40 is a structural component of the 40S ribosomal subunit, which is partially homologuos to prokaryotic ribosomal Protein S2 and has a long eukaryote-specific C-terminal region. In the present work, we have studied the binding of the Internal Ribosome Entry Site (IRES) of the hepatitis C virus (HCV) RNA to the 40S ribosomal subunit either deficient on Protein P40, or saturated with the recombinant P40, or pre-bound to monoclonal antibodies (MAB) 4F6 against P40. It was shown that the apparent association constant of HCV IRES binding to 40S subunits directly depends on P40 content in the subunits. Binding of MAB 4F6 against P40 to 40S subunits prevented the HCV IRES binding by the subunits and blocked translation of the IRES-containing RNA in cell-free translation system. The data obtained point to the involvement of the ribosomal Protein P40 in the binding of the HCV IRES by ribosomes and therefore in initiation of translation of RNA of this virus.
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Binding of human ribosomal Protein P40 and its truncated mutants to the small ribosomal subunit
Molecular Biology, 2008Co-Authors: Olga Kossinova, Alexey A. Malygin, E. S. Babailova, Galina G. KarpovaAbstract:Ribosomal Protein SA (rpSA), or P40, is a structural element of the small subunit of the eukaryotic ribosome. The N-terminal and central parts of rpSA are homologous to prokaryotic S2, whereas its C-terminal part is specific to eukaryotes. Preparations of 40S ribosomal subunits isolated from full-term human placenta proved to be deficient in SA to a varying extent. To study the rpSA binding to human 40S subunits, recombinant rpSA and its mutant forms with N-and C-terminal deletions were synthesized. The full-size and N-truncated rpSA variants bound to 40S subunits, while deletion of the C-terminal domain completely abolished the binding.
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Binding of human ribosomal Protein P40 and its truncated mutants to the small ribosomal subunit
Molekuliarnaia biologiia, 2008Co-Authors: O A Kosinova, Alexey A. Malygin, E S Babaĭlova, Galina G. KarpovaAbstract:Ribosomal Protein SA (rpSA) or P40 is a structural element of the small subunit of the eukaryotic ribosome. N-terminal and central parts of the Protein are homologous to prokaryotic rpS2 whereas its C-terminal part is eukaryote specific. In this study we showed that samples of 40S ribosomal subunits isolated from full-term human placenta are variably deficient in the rpSA content. To reveal rpSA ability to bind to human 40S ribosomal subunits, recombinant rpSA and its mutant forms with N- and C-terminal deletions have been synthesized. It was shown that both full-size and truncated from the N-terminus Proteins were able to bind to the 40S subunits whereas the mutant truncated from C-terminus was not.
Rainer Prohaska - One of the best experts on this subject based on the ideXlab platform.
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Characterization of P40/GPR69A as a peripheral membrane Protein related to the lantibiotic synthetase component C.
Biochemical and Biophysical Research Communications, 2000Co-Authors: Hemma Bauer, Herbert Mayer, Ulrich Salzer, Aron Marchler-bauer, Rainer ProhaskaAbstract:Abstract The 40 kDa erythrocyte membrane Protein P40/GPR69A, previously assigned to the G-Protein-coupled receptor superfamily, was now identified by peptide-antibodies and characterized as a loosely associated peripheral membrane Protein. This result is in striking contrast to the proposed seven-transmembrane Protein structure and function and therefore we wish to correct our previous proposal. P40 is located at the cytoplasmic side of the membrane and is neither associated with the cytoskeleton nor lipid rafts. Refined sequence analysis revealed that P40 is related to the LanC family of bacterial membrane-associated Proteins which are involved in the biosynthesis of antimicrobial peptides. Therefore, we rename P40 to LanC-like Protein 1 (LANCL1) and suggest that it may play a similar role as a peptide-modifying enzyme component in eukaryotic cells.
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characterization of P40 gpr69a as a peripheral membrane Protein related to the lantibiotic synthetase component c
Biochemical and Biophysical Research Communications, 2000Co-Authors: Hemma Bauer, Herbert Mayer, Ulrich Salzer, Aron Marchlerbauer, Rainer ProhaskaAbstract:The 40 kDa erythrocyte membrane Protein P40/GPR69A, previously assigned to the G-Protein-coupled receptor superfamily, was now identified by peptide-antibodies and characterized as a loosely associated peripheral membrane Protein. This result is in striking contrast to the proposed seven-transmembrane Protein structure and function and therefore we wish to correct our previous proposal. P40 is located at the cytoplasmic side of the membrane and is neither associated with the cytoskeleton nor lipid rafts. Refined sequence analysis revealed that P40 is related to the LanC family of bacterial membrane-associated Proteins which are involved in the biosynthesis of antimicrobial peptides. Therefore, we rename P40 to LanC-like Protein 1 (LANCL1) and suggest that it may play a similar role as a peptide-modifying enzyme component in eukaryotic cells.
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Isolation, molecular characterization, and tissue-specific expression of a novel putative G Protein-coupled receptor.
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1998Co-Authors: Herbert Mayer, Ulrich Salzer, Johannes Breuss, Sophie Ziegler, Aron Marchler-bauer, Rainer ProhaskaAbstract:We isolated a 40 kDa integral membrane Protein (P40) from human erythrocyte ghosts by affinity chromatography, using a C-terminal peptide of stomatin, and obtained partial sequences which enabled us to isolate two full-length cDNAs from human bone marrow and fetal brain cDNA libraries. The cDNA sequences were identical and encoded a novel putative G Protein-coupled receptor (399 amino acids). Northern and RNA dot blot analyses demonstrated that the major 4.8 kb-transcript is predominantly expressed in brain. In situ hybridization studies of tissue sections revealed high expression in neurons of the brain and spinal cord, in thymocytes, megakaryocytes, and macrophages.
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Short sequence-paper Isolation, molecular characterization, and tissue-specific expression of a novel putative G Protein-coupled receptor
1998Co-Authors: Herbert Mayer, Ulrich Salzer, Johannes Breuss, Sophie Ziegler, Aron Marchler-bauer, Rainer ProhaskaAbstract:We isolated a 40 kDa integral membrane Protein P40 from human erythrocyte ghosts by affinity chromatography, using a C-terminal peptide of stomatin, and obtained partial sequences which enabled us to isolate two full-length cDNAs from human bone marrow and fetal brain cDNA libraries. The cDNA sequences were identical and encoded a novel putative G . Protein-coupled receptor 399 amino acids . Northern and RNA dot blot analyses demonstrated that the major 4.8 kb-tran- script is predominantly expressed in brain. In situ hybridization studies of tissue sections revealed high expression in neurons of the brain and spinal cord, in thymocytes, megakaryocytes, and macrophages. q 1998 Elsevier Science B.V.
Y Kaneda - One of the best experts on this subject based on the ideXlab platform.
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analysis of nuclear localization of laminin binding Protein precursor P40 lbp P40
Biochemical and Biophysical Research Communications, 1996Co-Authors: M. Sato, Y Kaneda, K. Kinoshita, K. Tanaka, Yoshinaga Saeki, Akihiro IwamatsuAbstract:We isolated a monoclonal antibody M108, which recognized 40 kDa Protein (P40) in the cytoplasm, the perinuclear region in interphase and the perichromosomal region during mitosis. As reported previously, it was revealed from the immunofluorescent observation and the biochemical analyses that the nuclear P40 was associated both with the nuclear envelope and the chromatin DNA in interphase nuclei. In this report, we isolated the P40 from cytoplasmic particles, and identified it by extensive microsequencing as LBP/P40, which was considered to be a precursor of laminin binding Protein p67 (LBP/p67). Epitope-tagged LBP/P40 was expressed in cultured cells, and the Protein was localized in the nucleus as well as in the cytoplasm. Further analysis showed that the nuclear LBP/P40 was tightly associated with the nuclear structures.
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Analysis of Nuclear Localization of Laminin Binding Protein Precursor P40 (LBP/P40)
Biochemical and Biophysical Research Communications, 1996Co-Authors: M. Sato, Y Kaneda, K. Kinoshita, K. Tanaka, Yoshinaga Saeki, Akihiro IwamatsuAbstract:We isolated a monoclonal antibody M108, which recognized 40 kDa Protein (P40) in the cytoplasm, the perinuclear region in interphase and the perichromosomal region during mitosis. As reported previously, it was revealed from the immunofluorescent observation and the biochemical analyses that the nuclear P40 was associated both with the nuclear envelope and the chromatin DNA in interphase nuclei. In this report, we isolated the P40 from cytoplasmic particles, and identified it by extensive microsequencing as LBP/P40, which was considered to be a precursor of laminin binding Protein p67 (LBP/p67). Epitope-tagged LBP/P40 was expressed in cultured cells, and the Protein was localized in the nucleus as well as in the cytoplasm. Further analysis showed that the nuclear LBP/P40 was tightly associated with the nuclear structures.
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The Loss of 40-kDa Chromosomal Protein in Tuberous Sclerosis Lesions
Biochemical and Biophysical Research Communications, 1995Co-Authors: Mari Wataya-kaneda, Kae Hashimoto, Kunihiko Yoshikawa, Y KanedaAbstract:Tuberous sclerosis is an genetic disease characterized by systemic hamartomas. Some of the cultured cells derived from tuberous sclerosis show the distinct chromosomal disarrangement and abnormal cell division. To detect the Proteins responsible for this phenomenon, we investigated many nuclear components related to cell division. 40-kDa Protein (P40) recognized by one monoclonal antibody M108, which was present in nucleus, chromosomes and cytoplasm of many vertebrate culture cells, significantly decreased in the tuberous sclerosis cells. Immunoblot analysis revealed that in all the fractions the quantity of P40 of severe tuberous sclerosis cells was approximately 4 times less than P40 in normal fibroblasts.
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The analysis of 40 kDa nuclear Protein, P40, in interphase cells and mitotic cells
Journal of Cell Science, 1993Co-Authors: Y Kaneda, K. Kinoshita, M. Sato, K. TanakaAbstract:We previously reported that the monoclonal antibody M108 recognized a 40 kDa Protein both in the nucleus and the cytoplasm. This nuclear 40 kDa antigen was located in the nuclear envelope in interphase cells and in the perichromosomal region during mitosis. Now, we have analyzed this nuclear 40 kDa Protein (P40) further, through morphological and biochemical approaches. At the beginning of mitosis, the perinuclear P40 detached from the nuclear envelope and moved to surround the condensing chromatin, while in the late stage of mitosis, the perichromosomal P40 moved back to the reassembled nuclear envelope. Most of the perichromosomal P40 on the metaphase chromosome was solubilized only by DNase I treatment, not by either high salt or detergent treatment. On the other hand, the perinuclear P40 was not solubilized by DNase1 alone, or high salt detergent alone. Sequential treatments with DNase I and high salt detergent were required to extract P40 in interphase nuclei. These results suggest that P40 was associated both with the nuclear envelope and chromatin DNA in interphase nuclei, while it bound only to chromatin DNA in mitosis.
Steve Benson - One of the best experts on this subject based on the ideXlab platform.
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characterization and localized expression of the laminin binding Protein P40 lbp P40 gene during sea urchin development
Experimental Cell Research, 1995Co-Authors: Magdeleine Hung, Eric Rosenthal, Ben Boblett, Steve BensonAbstract:We have isolated and characterized the expression of a cDNA clone from the sea urchin Strongylocentrotus purpuratus that encodes a Protein very similar to LBP/P40, originally identified as a nonintegrin, 67-kDa laminin binding Protein. The deduced amino acid sequence of the Protein, which we call spLBP/P40, shows significant similarity with the LBP/P40 from other sources, although significant divergence does occur at the carboxyl end. The S. purpuratus mRNA is present as a maternal transcript and its level remains constant until activation of zygotic transcription at the hatching blastula stage, whereupon the total spLBP/P40 increases through the pluteus larval stage. Adult tissues also contain the spLBP/P40 mRNA. Both maternal and zygotic transcripts are translated as determined by their presence in polysomes. Immunoblot analysis using an antibody raised against a recombinant fusion Protein indicates that the concentration of the spLBP/P40 Protein remains constant during development despite the postblastula increase in mRNA concentration. However, the spatial distribution of the Protein changes from a uniform, intracellular distribution in all cells of cleavage and blastula stages to localized, elevated levels in cells of the gut, primary mesenchyme, and oral epithelium of prism larvae. The distribution of spLBP/P40 mRNA at different developmental stages, analyzed by in situ hybridization, reflects that of the Protein. Our results argue against a laminin binding function for this Protein; instead they place the spLBP/P40 gene in a class of previously described sea urchin genes involved in growth and proliferation.
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Characterization and localized expression of the laminin binding Protein/P40 (LBP/P40) gene during sea urchin development.
Experimental Cell Research, 1995Co-Authors: Magdeleine Hung, Eric Rosenthal, Ben Boblett, Steve BensonAbstract:We have isolated and characterized the expression of a cDNA clone from the sea urchin Strongylocentrotus purpuratus that encodes a Protein very similar to LBP/P40, originally identified as a nonintegrin, 67-kDa laminin binding Protein. The deduced amino acid sequence of the Protein, which we call spLBP/P40, shows significant similarity with the LBP/P40 from other sources, although significant divergence does occur at the carboxyl end. The S. purpuratus mRNA is present as a maternal transcript and its level remains constant until activation of zygotic transcription at the hatching blastula stage, whereupon the total spLBP/P40 increases through the pluteus larval stage. Adult tissues also contain the spLBP/P40 mRNA. Both maternal and zygotic transcripts are translated as determined by their presence in polysomes. Immunoblot analysis using an antibody raised against a recombinant fusion Protein indicates that the concentration of the spLBP/P40 Protein remains constant during development despite the postblastula increase in mRNA concentration. However, the spatial distribution of the Protein changes from a uniform, intracellular distribution in all cells of cleavage and blastula stages to localized, elevated levels in cells of the gut, primary mesenchyme, and oral epithelium of prism larvae. The distribution of spLBP/P40 mRNA at different developmental stages, analyzed by in situ hybridization, reflects that of the Protein. Our results argue against a laminin binding function for this Protein; instead they place the spLBP/P40 gene in a class of previously described sea urchin genes involved in growth and proliferation.
Alexey A. Malygin - One of the best experts on this subject based on the ideXlab platform.
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binding of the ires of hepatitis c virus rna to the 40s ribosomal subunit role of P40
Molecular Biology, 2009Co-Authors: Alexey A. Malygin, Olga Kossinova, E I Bondarenko, Valery B. Loktev, Z. V. Bochkaeva, Ivan N. Shatsky, Galina G. KarpovaAbstract:Ribosomal Protein P40 is a structural component of the eukaryotic 40S ribosomal subunit, is partly homologous to prokaryotic ribosomal Protein S2, and has a long eukaryote-specific C-terminal region. The internal ribosome entry site (IRES) of the hepatitis C virus (HCV) RNA was tested for the binding to 40S ribosomal subunits deficient in P40, saturated with recombinant P40, or pretreated with monoclonal antibody (MAB) 4F6 against P40. The apparent association constant of HCV IRES binding to 40S subunits was shown to directly depend on the P40 content in the subunits. MAB 4F6 prevented HCV IRES binding to 40S subunits and blocked translation of IRES-containing RNA in a cell-free translation system. The results implicate P40 in the binding of the HCV IRES to the ribosome and, therefore, in translation initiation on HCV RNA.
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Binding of the IRES of hepatitis C virus RNA to the 40S ribosomal subunit: role of Protein P40
Molekuliarnaia biologiia, 2009Co-Authors: Alexey A. Malygin, E I Bondarenko, Valery B. Loktev, Z. V. Bochkaeva, O A Kosinova, I N Shatskiĭ, Galina G. KarpovaAbstract:Ribosomal Protein P40 is a structural component of the 40S ribosomal subunit, which is partially homologuos to prokaryotic ribosomal Protein S2 and has a long eukaryote-specific C-terminal region. In the present work, we have studied the binding of the Internal Ribosome Entry Site (IRES) of the hepatitis C virus (HCV) RNA to the 40S ribosomal subunit either deficient on Protein P40, or saturated with the recombinant P40, or pre-bound to monoclonal antibodies (MAB) 4F6 against P40. It was shown that the apparent association constant of HCV IRES binding to 40S subunits directly depends on P40 content in the subunits. Binding of MAB 4F6 against P40 to 40S subunits prevented the HCV IRES binding by the subunits and blocked translation of the IRES-containing RNA in cell-free translation system. The data obtained point to the involvement of the ribosomal Protein P40 in the binding of the HCV IRES by ribosomes and therefore in initiation of translation of RNA of this virus.
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Binding of human ribosomal Protein P40 and its truncated mutants to the small ribosomal subunit
Molecular Biology, 2008Co-Authors: Olga Kossinova, Alexey A. Malygin, E. S. Babailova, Galina G. KarpovaAbstract:Ribosomal Protein SA (rpSA), or P40, is a structural element of the small subunit of the eukaryotic ribosome. The N-terminal and central parts of rpSA are homologous to prokaryotic S2, whereas its C-terminal part is specific to eukaryotes. Preparations of 40S ribosomal subunits isolated from full-term human placenta proved to be deficient in SA to a varying extent. To study the rpSA binding to human 40S subunits, recombinant rpSA and its mutant forms with N-and C-terminal deletions were synthesized. The full-size and N-truncated rpSA variants bound to 40S subunits, while deletion of the C-terminal domain completely abolished the binding.
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Binding of human ribosomal Protein P40 and its truncated mutants to the small ribosomal subunit
Molekuliarnaia biologiia, 2008Co-Authors: O A Kosinova, Alexey A. Malygin, E S Babaĭlova, Galina G. KarpovaAbstract:Ribosomal Protein SA (rpSA) or P40 is a structural element of the small subunit of the eukaryotic ribosome. N-terminal and central parts of the Protein are homologous to prokaryotic rpS2 whereas its C-terminal part is eukaryote specific. In this study we showed that samples of 40S ribosomal subunits isolated from full-term human placenta are variably deficient in the rpSA content. To reveal rpSA ability to bind to human 40S ribosomal subunits, recombinant rpSA and its mutant forms with N- and C-terminal deletions have been synthesized. It was shown that both full-size and truncated from the N-terminus Proteins were able to bind to the 40S subunits whereas the mutant truncated from C-terminus was not.
