Autoantibodies against a serine tRNA-protein complex implicated in cotranslational selenocysteine insertion.
AUTOR(ES)
Gelpi, C
RESUMO
We describe an autoantibody specificity present in a subgroup of patients with a severe form of autoimmune chronic active hepatitis. These antibodies precipitate a 90-nucleotide RNA from human whole cell extracts and recognize a 48-kDa polypeptide in immunoblotting assays. The RNA is a UGA suppressor serine tRNA that carries selenocysteine (tRNA[Ser]Sec)), as shown by sequence analysis. The protein does not appear to be seryl-tRNA synthetase; rather, it is an excellent candidate for a factor involved in cotranslational selenocysteine incorporation in human cells.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=50208Documentos Relacionados
- Direct tRNA-protein interactions in ribosomal complexes.
- Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis.
- An RNA-binding protein recognizes a mammalian selenocysteine insertion sequence element required for cotranslational incorporation of selenocysteine.
- Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon.
- Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria