Cleavage mechanism of ATP-dependent Lon protease toward ribosomal S2 protein.

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.
Authors	Wataru Nishii, Taichiro Suzuki, Mayumi Nakada, Yong-Tae Kim, Tomonari Muramatsu, Kenji Takahashi
Journal	FEBS letters (FEBS Lett) Vol. 579 Issue 30 Pg. 6846-50 (Dec 19 2005) ISSN: 0014-5793 [Print] England
PMID	16337203 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Escherichia coli Proteins Peptides Polyphosphates Recombinant Proteins Ribosomal Proteins ribosomal protein S2 sulA protein, E coli Adenosine Triphosphate Protease La
Topics	Adenosine Triphosphate (metabolism) Amino Acid Sequence Chromatography, Gel Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Escherichia coli (chemistry, enzymology, metabolism) Escherichia coli Proteins (chemistry, metabolism) Hydrolysis Hydrophobic and Hydrophilic Interactions Kinetics Mass Spectrometry Models, Molecular Molecular Sequence Data Molecular Weight Peptide Mapping Peptides (chemistry, metabolism) Polyphosphates (metabolism) Protease La (chemistry, metabolism) Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins (chemistry, metabolism) Ribosomal Proteins (chemistry, genetics, metabolism) Substrate Specificity Time Factors

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