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The primary structure of protein L17 from the Escherichia coli ribosome
Author(s) -
Rombauts Wilfried,
Feytons Valère,
Wittmann-Liebold Brigitte
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81124-1
Subject(s) - protein primary structure , thermolysin , peptide sequence , ribosomal protein , ribosome , biochemistry , trypsin , amino acid , protein subunit , chymotrypsin , chemistry , protease , protein sequencing , biology , cleavage (geology) , enzyme , rna , gene , paleontology , fracture (geology)
The complete sequence of protein L17 which is a component of the large subunit of the E. coli ribosome has been determined. Peptides deriving from enzymatic hydrolysis with trypsin, thermolysin, chymotrypsin and S. aureus and A. mellea protease were isolated and sequenced by the DABITC/PITC double coupling method. Some overlapping peptides were obtained after mild acid cleavage of the protein. According to the amino acid sequence protein L17 contains 127 residues and has a molecular mass of 14 365. The primary structure of protein L17 agrees well with the amino acid analysis of the intact protein and its N‐terminal sequence as derived from automatic sequencing in an improved Beckman sequencer. Secondary predictions and a search for homologous sequence stretches to other ribosomal proteins were made.