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40S Ribosomal Subunit

The Experts below are selected from a list of 300 Experts worldwide ranked by ideXlab platform

G G Karpova – 1st expert on this subject based on the ideXlab platform

  • Molecular environment of the subdomain IIIe loop of the RNA IRES element of hepatitis C virus on the human 40S Ribosomal Subunit
    Bioorganicheskaia khimiia, 2020
    Co-Authors: E S Laletina, A A Malygin, I N Shatskiĭ, D M Graĭfer, G G Karpova

    Abstract:

    The molecular environment of the internal ribosome entry site (IRES) element of hepatitis C viral (HCV) RNA in the binary complex with the human 40S Ribosomal Subunit was studied. To this end, RNA derivatives bearing mild UV-reactive perfluorophenylazide groups at nucleotide G87 in IRES domain II and at nucleotide A296 in the subdomain IIIe loop were used, which were prepared by the RNA complementarily-addressed modification with alkylating oligonucleotide derivatives. None of the RNA derivatives were shown to be crosslinked to the 18S rRNA of the 40S Subunit. It was found that the photoreactive group of IRES nucleotide A296 was crosslinked to the 40S Subunit S2/S3a, S5, and p40 (SOA) proteins. No protein crosslinking was observed for the RNA derivative containing the same photoreactive group in nucleotide G87. It was concluded that the subdomain IIIe loop of the HCV RNA IRES element in the complex with the 40S Subunit is located on the outer Subunit surface between the head and the body next to the “beak” near the entrance into the mRNA-binding channel. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2006, vol. 32, no. 3; see also http://www.maik.ru.

  • Binding of the IRES of hepatitis C virus RNA to the 40S Ribosomal Subunit: role of protein p40
    Molekuliarnaia biologiia, 2020
    Co-Authors: A A Malygin, Z V Bochkaeva, E I Bondarenko, O A Kosinova, V B Loktev, I N Shatskiĭ, G G Karpova

    Abstract:

    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.

  • Molecular environment of the IIId subdomain of the IRES element of hepatitits C virus RNA on the human 40S Ribosomal Subunit
    Bioorganicheskaia khimiia, 2020
    Co-Authors: E S Babaĭlova, A A Malygin, I N Shatskiĭ, D M Graĭfer, I Shtal, G G Karpova

    Abstract:

    The molecular environment of the key subdomain IIId of the internal ribosome entry site (IRES) element of hepatitis C virus (HCV) RNA in the binary complex with the human 40S Ribosomal Subunit was studied. To this end, HCV IRES derivatives bearing perfluorophenylazido groups activatable by mild UV at nucleotide G263 or A275 in the subdomain IIId stem were used. They were prepared by the complementarily addressed modification of the corresponding RNA transcript with alkylating oligodeoxynucleotide derivatives. None of the RNA derivatives were shown to be crosslinked to the 18S rRNA. It was found that the photoreactive groups of the IRES G263 and A275 nucleotides are crosslinked to Ribosomal proteins S3a, S14, and S16. For the IRES derivative with the photoreactive group in nucleotide G263, the degree of modification of proteins S14 and S16 was greater than that of S3a, whereas the derivative containing the same photoreactive group in nucleotide A275 was mainly crosslinked to proteins S3a and S14. An analysis of the data led to the conclusion that, in the binary complex of HCV IRES elements with the small Subunit of the 80S ribosome, its subdomain IIId stem is located on the outer Subunit surface between the head and the body next to the “beak” near the exit of mRNA from the ribosome.

A A Malygin – 2nd expert on this subject based on the ideXlab platform

  • Molecular environment of the subdomain IIIe loop of the RNA IRES element of hepatitis C virus on the human 40S Ribosomal Subunit
    Bioorganicheskaia khimiia, 2020
    Co-Authors: E S Laletina, A A Malygin, I N Shatskiĭ, D M Graĭfer, G G Karpova

    Abstract:

    The molecular environment of the internal ribosome entry site (IRES) element of hepatitis C viral (HCV) RNA in the binary complex with the human 40S Ribosomal Subunit was studied. To this end, RNA derivatives bearing mild UV-reactive perfluorophenylazide groups at nucleotide G87 in IRES domain II and at nucleotide A296 in the subdomain IIIe loop were used, which were prepared by the RNA complementarily-addressed modification with alkylating oligonucleotide derivatives. None of the RNA derivatives were shown to be crosslinked to the 18S rRNA of the 40S Subunit. It was found that the photoreactive group of IRES nucleotide A296 was crosslinked to the 40S Subunit S2/S3a, S5, and p40 (SOA) proteins. No protein crosslinking was observed for the RNA derivative containing the same photoreactive group in nucleotide G87. It was concluded that the subdomain IIIe loop of the HCV RNA IRES element in the complex with the 40S Subunit is located on the outer Subunit surface between the head and the body next to the “beak” near the entrance into the mRNA-binding channel. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2006, vol. 32, no. 3; see also http://www.maik.ru.

  • Binding of the IRES of hepatitis C virus RNA to the 40S Ribosomal Subunit: role of protein p40
    Molekuliarnaia biologiia, 2020
    Co-Authors: A A Malygin, Z V Bochkaeva, E I Bondarenko, O A Kosinova, V B Loktev, I N Shatskiĭ, G G Karpova

    Abstract:

    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.

  • Molecular environment of the IIId subdomain of the IRES element of hepatitits C virus RNA on the human 40S Ribosomal Subunit
    Bioorganicheskaia khimiia, 2020
    Co-Authors: E S Babaĭlova, A A Malygin, I N Shatskiĭ, D M Graĭfer, I Shtal, G G Karpova

    Abstract:

    The molecular environment of the key subdomain IIId of the internal ribosome entry site (IRES) element of hepatitis C virus (HCV) RNA in the binary complex with the human 40S Ribosomal Subunit was studied. To this end, HCV IRES derivatives bearing perfluorophenylazido groups activatable by mild UV at nucleotide G263 or A275 in the subdomain IIId stem were used. They were prepared by the complementarily addressed modification of the corresponding RNA transcript with alkylating oligodeoxynucleotide derivatives. None of the RNA derivatives were shown to be crosslinked to the 18S rRNA. It was found that the photoreactive groups of the IRES G263 and A275 nucleotides are crosslinked to Ribosomal proteins S3a, S14, and S16. For the IRES derivative with the photoreactive group in nucleotide G263, the degree of modification of proteins S14 and S16 was greater than that of S3a, whereas the derivative containing the same photoreactive group in nucleotide A275 was mainly crosslinked to proteins S3a and S14. An analysis of the data led to the conclusion that, in the binary complex of HCV IRES elements with the small Subunit of the 80S ribosome, its subdomain IIId stem is located on the outer Subunit surface between the head and the body next to the “beak” near the exit of mRNA from the ribosome.

Ulrike Kutay – 3rd expert on this subject based on the ideXlab platform

  • usp16 counteracts mono ubiquitination of rps27a and promotes maturation of the 40S Ribosomal Subunit
    eLife, 2020
    Co-Authors: Christian Montellese, Ivo Zemp, Stefanie Jonas, Jasmin Van Den Heuvel, Caroline Ashiono, Kerstin Dorner, Andre Melnik, Paola Picotti, Ludovic C Gillet, Ulrike Kutay

    Abstract:

    Establishment of translational competence represents a decisive cytoplasmic step in the biogenesis of 40S Ribosomal Subunits. This involves final 18S rRNA processing and release of residual biogenesis factors, including the protein kinase RIOK1. To identify novel proteins promoting the final maturation of human 40S Subunits, we characterized pre-Ribosomal Subunits trapped on RIOK1 by mass spectrometry, and identified the deubiquitinase USP16 among the captured factors. We demonstrate that USP16 constitutes a component of late cytoplasmic pre-40S Subunits that promotes the removal of ubiquitin from an internal lysine of Ribosomal protein RPS27a/eS31. USP16 deletion leads to late 40S Subunit maturation defects, manifesting in incomplete processing of 18S rRNA and retarded recycling of late-acting ribosome biogenesis factors, revealing an unexpected contribution of USP16 to the ultimate step of 40S synthesis. Finally, ubiquitination of RPS27a appears to depend on active translation, pointing at a potential connection between 40S maturation and protein synthesis.

  • human aatf che 1 forms a nucleolar protein complex with ngdn and nol10 required for 40S Ribosomal Subunit synthesis
    Nucleic Acids Research, 2016
    Co-Authors: Lukas Bammert, Stefanie Jonas, Rosemarie Ungricht, Ulrike Kutay

    Abstract:

    Mammalian AATF/Che-1 is essential for embryonic development, however, the underlying molecular mechanism is unclear. By immunoprecipitation of human AATF we discovered that AATF forms a salt-stable protein complex together with neuroguidin (NGDN) and NOL10, and demonstrate that the AATF-NGDN-NOL10 (ANN) complex functions in ribosome biogenesis. All three ANN complex members localize to nucleoli and display a mutual dependence with respect to protein stability. Mapping of protein-protein interaction domains revealed the importance of both the evolutionary conserved WD40 repeats in NOL10 and the UTP3/SAS10 domain in NGDN for complex formation. Functional analysis showed that the ANN complex supports nucleolar steps of 40S Ribosomal Subunit biosynthesis. All complex members were required for 18S rRNA maturation and their individual depletion affected the same nucleolar cleavage steps in the 5′ETS and ITS1 regions of the Ribosomal RNA precursor. Collectively, we identified the ANN complex as a novel functional module supporting the nucleolar maturation of 40S Ribosomal Subunits. Our data help to explain the described role of AATF in cell proliferation during mouse development as well as its requirement for malignant tumor growth.

  • Human AATF/Che-1 forms a nucleolar protein complex with NGDN and NOL10 required for 40S Ribosomal Subunit synthesis
    Nucleic Acids Research, 2016
    Co-Authors: Lukas Bammert, Stefanie Jonas, Rosemarie Ungricht, Ulrike Kutay

    Abstract:

    Mammalian AATF/Che-1 is essential for embryonic development, however, the underlying molecular mechanism is unclear. By immunoprecipitation of human AATF we discovered that AATF forms a salt-stable protein complex together with neuroguidin (NGDN) and NOL10, and demonstrate that the AATF-NGDN-NOL10 (ANN) complex functions in ribosome biogenesis. All three ANN complex members localize to nucleoli and display a mutual dependence with respect to protein stability. Mapping of protein-protein interaction domains revealed the importance of both the evolutionary conserved WD40 repeats in NOL10 and the UTP3/SAS10 domain in NGDN for complex formation. Functional analysis showed that the ANN complex supports nucleolar steps of 40S Ribosomal Subunit biosynthesis. All complex members were required for 18S rRNA maturation and their individual depletion affected the same nucleolar cleavage steps in the 5′ETS and ITS1 regions of the Ribosomal RNA precursor. Collectively, we identified the ANN complex as a novel functional module supporting the nucleolar maturation of 40S Ribosomal Subunits. Our data help to explain the described role of AATF in cell proliferation during mouse development as well as its requirement for malignant tumor growth.