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Cloning and sequence analysis of cDNA for the proteasome activator PA28-β subunit of flounder ( Paralichthys olivaceus)

Proteasome is a large multisubunit complex involved in intracellular proteolysis in antigen processing for loading MHC class I molecules. Two activators PA28-α and PA28-β, which are induced by interferon-γ (IFN-γ), activate this latent enzyme complex. Genes encoding these activators, PMSE1 and PMSE2...

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Bibliographic Details
Published in:Molecular immunology 2003-12, Vol.40 (9), p.611-616
Main Authors: Kim, Dae-Hyun, Lee, Sun-Me, Hong, Bo-Young, Kim, Young-Tae, Choi, Tae-Jin
Format: Article
Language:English
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Summary:Proteasome is a large multisubunit complex involved in intracellular proteolysis in antigen processing for loading MHC class I molecules. Two activators PA28-α and PA28-β, which are induced by interferon-γ (IFN-γ), activate this latent enzyme complex. Genes encoding these activators, PMSE1 and PMSE2, respectively, have been characterized from various mammalian but only from zebrafish among piscine. We have cloned a PSME2 gene homologue from a leukocyte cDNA library of flounder, a marine fish. The flounder PSME2 gene (fPSME2) encompasses 1063 nucleotides and encodes a polypeptide of 242 amino acids (aa), with a deduced molecular weight of 27.2 kDa. The deduced protein has 82% sequence similarity to that of zebrafish and 73–74% sequence similarity to that of various mammalians and shows higher level sequence homology in the C-terminal region. There was a PA28-β protein subunit-specific insert located at the corresponding to the KEKE motif of PA28-α protein. A phylogenetic tree derived using deduced amino acid sequences showed a diversion of piscine PSME2 from mammalian counterpart after diversion of PSME1 and PSME2 from a common ancestral gene. Northern blot analysis revealed a higher level expression of fPSME2 gene in kidney, spleen and muscle tissues of bacterial lipopolysaccharide (LPS) stimulated flounder than those from non-induced flounder.
ISSN:0161-5890
1872-9142
DOI:10.1016/j.molimm.2003.08.005