作者: Norbert Wedel , Susanne Clausmeyer , Reinhold G. Herrmann , Laura Gardet-Salvi , Peter Sch�rmann
DOI: 10.1007/BF00040668
关键词: Amino acid 、 Complementary DNA 、 Gene 、 Nucleic acid sequence 、 Expression vector 、 Peptide sequence 、 Sequence alignment 、 Molecular biology 、 Biochemistry 、 Biology 、 Thioredoxin
摘要: Using the expression vector λgt11 and immunochemical detection, six cDNA clones that encode entire precursor polypeptides for spinach thioredoxin m were isolated characterized. The ca. 1.0 kb sequence of largest clone hybridizes to an RNA species 1.1 kb. In each instance sequences display single open reading frames encoding 181 amino acid residues corresponding a molecular mass 19.8 kDa. independently selected cDNAs fall into two classes are indicative at least (closely related) genes this protein. deduced from differ some extent published m. predict identical mature proteins 112–114 acids polypeptide 12.4–12.6 kDa, include stroma-targeting N-terminal transit peptides 67 which removed during or after import organelle. Precursor protein was made in vitro different imported intact chloroplasts. Independent used, isoforms detected chloroplasts instance. They comigrated with authentic mb mc. These results indicate size variants observed vivo result post-translational modification do not originate genes.