Subunit Composition and Cleavage Specificity in Phenotype-Dependent Differences in Proteasome
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Infection with Salmonella typhimurium has no effect on the composition and cleavage specificity of the 20S proteasome in human lymphoid cells.
Human leucocyte antigen (HLA)-B27 is strongly associated with spondyloarthropathies, including reactive arthritis. Several Gram-negative bacteria, such as Salmonella typhimurium, can trigger this disease. It has been suggested that peptides derived from bacterial proteins and presented by HLA-B27 to cytotoxic T lymphocytes might show molecular mimicry with autologous peptides, leading to T-cell...
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Proteinase yscE, the yeast proteasome, is a member of the nonlysosomal, high molecular mass (approximately 700 kDa) multifunctional proteinase complexes that are highly conserved from yeast to man. We have isolated mutants defective in one of the three proteolytic activities of the enzyme complex, i.e. in cleavage of peptide bonds after acidic amino acids. Using one of these mutants (pre4-1), w...
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PA28 § / g is a regulatory complex of the 20S proteasome which consists of two IFN+ inducible subunits. Both subunits, § and g , contribute equally to the formation of hexaor heptameric rings which can associate with the 20S proteasome. Previously, we have shown that overexpression of the PA28 § subunit enhanced the MHC class I-restricted presentation of two viral epitopes and that purified PA2...
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expressed in immune tissues and are expressed at much lower levels in other cell types. Immunoproteasomes play a major role in antigen presentation on MHC class I. These proteasomes, while of similar efficiency to the standard or constitutive proteasome, have different cleavage preferences so that the spectrum of antigenic peptides produced differs from that seen with the standard proteasome in...
متن کاملInterferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
The proteasome is a 700-kD multisubunit enzyme complex with several proteolytically active sites. The enzyme complex is involved in both ubiquitin-dependent and -independent protein degradation and may contribute to the processing of antigens presented by major histocompatibility complex (MHC) class I molecules. Here we demonstrate that treatment of mouse fibroblast cells with 20 U interferon g...
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تاریخ انتشار 1998