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Cleavage mechanism of ATP‐dependent Lon protease toward ribosomal S2 protein
Author(s) -
Nishii Wataru,
Suzuki Taichiro,
Nakada Mayumi,
Kim Yong-Tae,
Muramatsu Tomonari,
Takahashi Kenji
Publication year - 2005
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/j.febslet.2005.11.026
Subject(s) - cleavage (geology) , protease , ribosomal protein , chemistry , polyphosphate , enzyme , ribosomal rna , biochemistry , stereochemistry , biophysics , biology , ribosome , rna , phosphate , paleontology , fracture (geology) , gene
The Escherichia coli ATP‐dependent protease Lon degrades ribosomal S2 protein in the presence of inorganic polyphosphate (polyP). In this study, the process of the degradation was investigated in detail. During the degradation, 68 peptides with various sizes (4–29 residues) were produced in a processive fashion. Cleavage occurred at 45 sites, whose P 1 and P 3 positions were dominantly occupied by hydrophobic residues. These cleavage sites were located preferentially at the regions with rigid secondary structures and the P 1 residues of the major cleavage sites appeared to be concealed from the surface of the substrate molecule. Furthermore, polyP changed not only the substrate preference but also the oligomeric structure of the enzyme.