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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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Published in: | Molecular immunology 2003-12, Vol.40 (9), p.611-616 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0161-5890 1872-9142 |
DOI: | 10.1016/j.molimm.2003.08.005 |