Identification of an amino acid-regulated mRNA from rat liver as the mammalian equivalent of bacterial ribosomal protein L22.
作者： R.O. Laine , P.J. Laipis , N.F. Shay , M.S. Kilberg
DOI: 10.1016/S0021-9258(19)47324-9
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摘要: Amino acid deprivation of rat hepatoma cells induced the levels a 612-base pair mRNA termed ASI (Shay, N. F., Nick, H. S., and Kilberg, M. S. (1990) J. Biol. Chem. 265, 17844-17848). The was present at equal to or greater than actin in every tissue tested. corresponding full-length cDNA cloned, report demonstrates that deduced 184-residue amino sequence shares 30% identity number bacterial chloroplast L22 ribosomal proteins, including those from Escherichia coli Halobacterium halobium. A monospecific anti-peptide antibody produced upon immunochemical analysis subcellular fractions liver recognized band microsomal fraction and, more specifically, reacted with single polypeptide large subunit fraction. did not react any proteins mitochondrial subunit, but recognize protein human homogenate same relative mobility (23 kDa) as observed for liver.
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