Abstract:
:The immunoproteasome subunit low molecular weight protein 2 (LMP2) codon 60 polymorphism has been associated with autoimmune diseases. It has also been demonstrated to influence susceptibility to TNF-alpha-induced apoptosis in blood cells and proteasome activity in aged human brain. In the present study, an in silico model of immunoproteasome was used to examine the effect of the R60H polymorphism in the LMP2 subunit. The investigation of immunoproteasome expression, activity and intracellular localisation in an in vitro cellular model, namely lymphoblastoid cell lines, showed no major variations in functionality and amount, while a significant difference in antibody affinity was apparent. These data were integrated with previous results obtained in different tissues and combined with a structural model of the LMP2 polymorphism. Accordingly, we identified three prospective mechanisms that could explain the biological data for the polymorphism, such as modulation of the binding affinity of a putative non-catalytic modifier site on the external surface of the immunoproteasome core, or the modification of any channel between alpha and beta rings.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Mishto M,Santoro A,Bellavista E,Sessions R,Textoris-Taube K,Dal Piaz F,Carrard G,Forti K,Salvioli S,Friguet B,Kloetzel PM,Rivett AJ,Franceschi Cdoi
10.1515/BC.2006.056subject
Has Abstractpub_date
2006-04-01 00:00:00pages
417-29issue
4eissn
1431-6730issn
1437-4315journal_volume
387pub_type
杂志文章abstract::In bacteria, UGA stop codons can be recoded to direct the incorporation of selenocysteine into proteins on the ribosome. Recoding requires a selenocysteine incorporation sequence (SECIS) downstream of the UGA codon, a specialized translation factor SelB, and the non-canonical Sec-tRNASec, which is formed from Ser-tRNA...
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