Autoantibodies against a serine tRNA-protein complex implicated in cotranslational selenocysteine insertion.
C Gelpi, EJ Sontheimer… - Proceedings of the …, 1992 - pnas.org
C Gelpi, EJ Sontheimer, JL Rodriguez-Sanchez
Proceedings of the National Academy of Sciences, 1992•pnas.orgWe 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 …
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 …
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.
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