PMID:16337203
| Citation |
Nishii, W, Suzuki, T, Nakada, M, Kim, YT, Muramatsu, T and Takahashi, K (2005) Cleavage mechanism of ATP-dependent Lon protease toward ribosomal S2 protein. FEBS Lett. 579:6846-50 |
|---|---|
| Abstract |
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 P1 and P3 positions were dominantly occupied by hydrophobic residues. These cleavage sites were located preferentially at the regions with rigid secondary structures and the P1 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. |
| Links |
PubMed Online version:10.1016/j.febslet.2005.11.026 |
| Keywords |
Adenosine Triphosphate/metabolism; Amino Acid Sequence; Chromatography, Gel; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrolysis; Hydrophobic and Hydrophilic Interactions; Kinetics; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Molecular Weight; Peptide Mapping; Peptides/chemistry; Peptides/metabolism; Polyphosphates/metabolism; Protease La/chemistry; Protease La/metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Ribosomal Proteins/chemistry; Ribosomal Proteins/genetics; Ribosomal Proteins/metabolism; Substrate Specificity; Time Factors |
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