ZHANG Bo, WANG Xianli, SONG Wenping, ZHENG debin, MA Chao, XIAO Guangxia, Jia Lei. Cloning, characterization, and expression of a novel member of proteasomal subunits gene in turbot, Scophthalmus maximus[J]. Acta Oceanologica Sinica, 2015, 34(1): 110-118. doi: 10.1007/s13131-015-0586-y
Citation: ZHANG Bo, WANG Xianli, SONG Wenping, ZHENG debin, MA Chao, XIAO Guangxia, Jia Lei. Cloning, characterization, and expression of a novel member of proteasomal subunits gene in turbot, Scophthalmus maximus[J]. Acta Oceanologica Sinica, 2015, 34(1): 110-118. doi: 10.1007/s13131-015-0586-y

Cloning, characterization, and expression of a novel member of proteasomal subunits gene in turbot, Scophthalmus maximus

doi: 10.1007/s13131-015-0586-y
  • Received Date: 2013-08-18
  • Rev Recd Date: 2014-04-18
  • The proteasome is a large, polymeric protease complex responsible for the degradation of intracellular proteins and generation of peptides that bind to class I major histocompatibility complex (MHC) molecules. This study identified a new member of proteasomal subunits in turbots (Scophthalmus maximus). The fulllength cdNA sequence of turbot proteasomal subunit was obtained. Sequence analysis indicated that its primary structure is highly similar to that of LMP7 from other vertebrates. The relationship between the turbot LMP7 expression and immune responses to pathogen infection was reported. Quantitative reverse transcriptase polymerase chain reaction showed that LMP7 was expressed differently in various tissues, with higher expression in the spleen, liver, muscle, and skin. The LMP7 expression was the highest at 96 h after challenge with lymphocyctis disease virus (LCdV) and at 12 h after challenge with Vibrio anguillarum in the turbot liver, kidney, and spleen. Furthermore, the LMP7 expression distinctly increased in turbot kidney cells at 24 h after challenge with V.anguillarum and at 96 h after challenge with LCdV. These results indicate that the turbot LMP7 protein participates in immune responses and may play a significant role in the immune process.
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  • Aki M, Shimbara N, Takashina M, et al. 1994. Interferon-gamma induces different subunit organizations and functional diversity of proteasomes. J Biochem, 115(2): 257-269
    Akiyama K, Kagawa S, Tamura T, et al. 1994a. Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-γ for acquirement of the functional diversity responsible for antigen processing. FEBS Lett, 343(1): 85-88
    Akiyama K, Yokota K, Kagawa S, et al. 1994b. cdNA cloning and interferon-gamma down-regulation of proteasomal subunits X and Y. Science, 265(5176): 1231-1234
    Arnold d, driscoll J, Androlewicz M, et al. 1992. Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules. Nature, 360(6400): 171-174
    Baumeister W, Walz J, Zühl F, et al. 1998. The proteasome: paradigm of a self-compartmentalizing protease. Cell, 92(3): 367-380
    Braun R E. 2000. Temporal control of protein synthesis during spermatogenesis. Int J Androl, 23(S2): 92-94
    Brown M G, driscoll J, Monaco J J. 1991. Structural and serological similarity of MHC linked LMP and proteasome (multicatalytic proteinase) complexes. Nature, 353(6342): 355-357
    Chen Songlin, Hong Yunhan, Scherer S, et al. 2001. Lack of ultraviolet-light inducibility of the medakafish (Oryzias latipes) tumor suppressor gene p53. Gene, 264(2): 197-203
    Chen Songlin, Xu Meiyu, Hu Songnan, et al. 2004. Analysis of immune-relevant genes expressed in red sea bream (Chrysophrys major) spleen. Aquaculture, 240(1-4): 115-130
    Childers C P, Newkirk H L, Honeycutt d A, et al. 2005. Comparative analysis of the bovine MHC class IIb sequence identifies inversion breakpoints and three unexpected genes. Anim Genet, 37(2): 121-129
    Clark M S, Pontarotti P, Gilles A, et al. 2000. Identification and characterization of a β Proteasome subunit cluster in the Japanese Pufferfish (Fugu rubripes). J Immunol, 165(8): 4446-4452
    Clustal W. 1994. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucl Acid Res, 22(22): 4673-4680
    dayhoff M O, Schwartz R M, Orcutt B C. 1978. A model of evolutionary change in protein. In: dayhoff M O, ed. Atlas of Protein Sequence and Structure. Washington dC: National Biomedical Research Foundation, 345-358
    dick L R, Aldrich C, Jameson S C, et al. 1994. Proteolytic processing of ovalbumin and beta-galactosidase by the proteasome to yield antigenic peptides. J Immunol, 152(8): 3884-3894
    driscoll J, Brown M G, Finley d, et al. 1993. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature, 365(6443): 262-267
    Eleuteri A M, Kohanski R A, Cardozo C, et al. 1997. Bovine spleen multicatalytic proteinase complex (proteasome) replacement of X, Y, and Z subunits by LMP7, LMP2 and MECL1 and changes in properties and specificity. J Biol Chem, 272(18): 11824-11831
    Fehling H J, Swat W, Laplace C, et al. 1994. MHC class I expression in mice lacking the proteasome subunit LMP-7. Science, 265(5176): 1234-1237
    Früh K, Gossen M, Wang K, et al. 1994. displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. J EMBO, 13(14): 3236-3244
    Gaczynska M, Rock K L, Goldberg A L. 1993. Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature, 365(6443): 264-267
    Griffin T A, Nandi d, Cruz M, et al. 1998. Immunoproteasome assembly: cooperative incorporation of interferon γ (IFN-γ)-inducible subunits. J Exp Med, 187(1): 97-104
    Groettrup M S, Khan K, Schwarz G, et al. 2001. Interferon-γ inducible exchanges of 20S proteasome active site subunits: why? Biochimie, 83: 367-372
    Groettrup M R, Kraft S, Kostka S, et al. 1996. A third interferon-γ induced subunit exchange in the 20 S proteasome. Eur J Immunol, 26(4): 863-869
    Groll M, ditzel L, Löwe J, et al. 1997. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature, 386(6624): 463-471
    Hallermalm K, Seki K, Wei C, et al. 2001. Tumor necrosis factor-alpha induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface. Blood, 98(4): 1108-1115
    Khan S, Broek M, Schwartz K, et al. 2001. Immuno proteasomes largely replace constitutive proteasomes during an antiviral and antibacterial immune responses in the liver. J Immunol, 167(12): 6859-6868
    Kloetzel P M, Ossendorp F. 2004. Proteasome and peptidase function in MHC-class I-mediated antigen presentation. Curr Opin Immunol, 16(1): 76-81
    Kopp F, Steiner R, dahlmann B, et al. 1986. Size and shape of the multicatalytic proteinase from rat skeletal muscle. Biochim Biophys Acta, 872(3): 253-260
    Kumar S, Tamura K, Nei M, et al. 2004. Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform, 5(2): 150-163
    Leong J S, Jantzen S G, Kristian R, et al. 2010. Salmo salar and Esox lucius full-length cdNA sequences reveal changes in evolutionary pressures on a post-tetraploidization genome. BMC Genomics, 11(1): 279-296
    Lindenstrom T, Secombes C J, Buchmann K. 2004. Expression of immune response genes in rainbow trout skin induced by Gyrodactylus derjavini infections. Vet Immunol Immunopathol, 97(3-4): 137-148
    Liu Yang, Chen Songlin, Meng Liang, et al. 2007. Cloning, characterization and expression analysis of a CXCL10-like chemokine from turbot (Scophthalmus maximus). Aquaculture, 272(1-4): 199-207
    Livak K J, Schmittgen T d. 2001. Analysis of relative gene expression data using real time quantitative PCR and the 2-ΔΔt method. Methods, 25(4): 402-408
    Loukissa A, Cardozo C, Altschuller-Felberg C, et al. 2000. Control of LMP7 expression in human endothelial cells by cytokines regulating cellular and humoral immunity. Cytokine, 12(9): 1326-1330
    Mayumi I, Nonaka M. 2010. Evolutionary analysis of two classical MHC class I loci of the medaka fish, Oryzias latipes: haplotype-specific genomic diversity, locus-specific polymorphisms and interlocus homogenization. Immunogenetics, 62(5): 319-332
    Mehta R B, Nonaka M I, Nonaka M. 2009. Comparative genomic analysis of the major histocompatibility complex class I region in the teleost genus Oryzias. Immunogenetics, 61(5): 385-399
    Miura F, Tsukamoto K, Mehta R B, et al. 2010. Transspecies dimorphic allelic lineages of the proteasome subunit beta-type 8 gene (PSMB8) in the teleost genus Oryzias. Proc Natl Acad Sci USA, 107(50): 21599-604
    Monaco J J, Cho S, Attaya M. 1990. Transport protein genes in the murine MHC: possible implications for antigen processing. Science, 250(4988): 1723-1726
    Monaco J J, Nandi d. 1995. The genetics of proteasomes and antigen processing. Ann Rev Gen, 29(1): 729-754
    Morten F, Lukacs d, Harstad H, et al. 2007. Genomic organization of duplicated major histocompatibility complex class I regions in Atlantic salmon (Salmo salar). BMC Gen, 8(1): 251-256
    Murray B W, Holger S, Klein J. 1999. Analysis of a 26-kb region linked to the MHC in Zebrafish: Genomic organization of the proteasome component β/transporter associated with antigen processing-2 gene cluster and identification of five new proteasome β Subunit genes. J Immunol, 163(5): 2657-2666
    Nandi d, Woodward E, Ginsburg d B, et al. 1997. Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor β subunits. EMBO J, 16(17): 5363-5375
    Nelson J E, Loukissa A, Altschuller-Felberg C, et al. 2000. Up-regulation of the proteasome subunit LMP7 in tissues of endotoxemic rats. J Lab Clin Med, 135(4): 324-331
    Noda C, Tanahashi N, Shimbara N, et al. 2000. Tissue distribution of constitutive proteasomes immunoproteasomes and PA28 in rats. Biochem Biophys Res Commun, 277(2): 348-354
    Ortiz-Navarrete V, Seelig A, Gernold M, et al. 1991. Subunit of the '20S' proteasome (multicatalytic proteinase) encoded by the major histocompatibility complex. Nature, 353(6345): 662-664
    Puhler G, Weinkauf S, Bachmann L, et al. 1992. Subunit stoichiometry and three-dimensional arrangement in proteasomes from thermoplasma acidophilum. EMBO J, 11(4): 1607-1616
    Rock K, Gramm L C, Rothstein L, et al. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell, 78(5): 761-771
    Saitou N, Nei M. 1987. The neighbour-joining method: a new method for reconstructing phylogenetic trees. Mol Bio Evol, 4(4): 406-425
    Tanaka K. 1994. Role of proteasomes modified by interferon gamma in antigen processing. J Leuk Biol, 56(5): 571-575
    Tanaka K. 1998. Proteasomes: structure and biology. J Biochem, 123(2): 195-204
    Tanaka K, Ichihara A. 1989. Autodegradation of rat liver proteasomes (large multicatalytic proteinase complexes). Biochem Biophys Res Commun, 158(2): 548-554
    Tanaka K, Yoshimura T, Kumatori A, et al. 1988. Proteasomes (multi-protease complexes) as 20S ring-shaped particles in a variety of eukaryotic cells. J Biol Chem, 263(31): 16209-16217
    Tsukamoto K, Sakaizumi M, Hata M, et al. 2009. dichotomous haplotypic lineages of the immunoproteasome subunit genes, PSMB8 and PSMB10, in the MHC class I region of a Teleost Medaka, Oryzias latipes. Mol Biol Evol, 26(4): 769-781
    Wilk S, Orlowski M. 1980. Cation-sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary enzyme. J Neurochem, 35(5): 1172-1182
    Xu Hongtao, Piao Chunai, Jiang Zhongliang, et al. 2000. Study on the causative agent of lymphocystic disease in cultured flounder, Paralichthys Olivaceus, in mainland China. Chi J Virol (in Chinese), 16(3): 223-226
    Yang Y, Waters J B, Fruh K, et al. 1992. Proteasomes are regulated by interferon gamma: implications for antigen processing. Proc Natl Acad Sci USA, 89(11): 4928-4932
    Yewdell J, Lapham C, Bacik I, et al. 1994. MHC-encoded proteasome subunits LMP2 and LMP7 are not required for efficient antigen presentation. J Immunol, 152(3): 1163-1170
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