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The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes
Author(s) -
Brosius Jürgen,
Chen Robert
Publication year - 1976
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(76)80415-2
Subject(s) - ribosome , chen , physics , escherichia coli , center (category theory) , stereochemistry , chemistry , genetics , biology , crystallography , rna , ecology , gene
Protein L16 from the large ribosomal subunit of E. coli binds directly to the 23s RNA [l] . Reconstitution experiments [2,3] and affinity labelling studies [4,5] demonstrated that L16 is involved in chloramphenicol binding and, thus, is located at the A-site of the peptidyltransferase center. Furthermore, affinity labelling experiments using modified Phe-tRNA [6,7] and inhibition experiments with antibodies [8] also showed that this protein is part of, or in the neighbourhood of, the peptidyltransferase center. Finally, from reconstitution experiments it was concluded that this protein may itself exert the peptidyltransferase activity [9]. The elucidation of the amino acid sequence of this functionally important protein is essential to obtain a further insight at the molecular level into those events which are associated with peptidyltransferase activity. In determining the primary structure of L16 we have used refined micro techniques that have been developed in determining the primary structures of proteins S9, L18, L27 and L34 [lo-131 and that have been described in detail elsewhere [ 141. The analysis of protein L16 is a further example of the quality and feasibility of these micro techniques.