NDLI: ATP-dependent Degradation of CcdA by Lon Protease EFFECTS OF SECONDARY STRUCTURE AND HETEROLOGOUS SUBUNIT INTERACTIONS

Content Provider	Journal of Biological Chemistry (JBC)
Author	Melderen, Laurence Van Thi, Minh Hoa Dao Lecchi, Paolo Gottesman, Susan Couturier, Martine Maurizi, Michael R.
Abstract	CcdA, the antidote protein of the ccd post-segregational killing system carried by the F plasmid, was degraded in vitro by purified Lon protease from Escherichia coli. CcdA had a low affinity for Lon (Km ≥200 µM), and the peptide bond turnover number was ∼10 min−1. CcdA formed tight complexes with purified CcdB, the killer protein encoded in the ccd operon, and fluorescence and hydrodynamic measurements suggested that interaction with CcdB converted CcdA to a more compact conformation. CcdB prevented CcdA degradation by Lon and blocked the ability of CcdA to activate the ATPase activity of Lon, suggesting that Lon may recognize bonding domains of proteins exposed when their partners are absent. Degradation of CcdA required ATP hydrolysis; however, CcdA41, consisting of the carboxyl-terminal 41 amino acids of CcdA and lacking the α-helical secondary structure present in CcdA, was degraded without ATP hydrolysis. Lon cleaved CcdA primarily between aliphatic and hydrophilic residues, and CcdA41 was cleaved at the same peptide bonds, indicating that ATP hydrolysis does not affect cleavage specificity. CcdA lost α-helical structure at elevated temperatures (Tm ∼50°C), and its degradation became independent of ATP hydrolysis at this temperature. ATP hydrolysis may be needed to disrupt interactions that stabilize the secondary structure of proteins allowing the disordered protein greater access to the proteolytic active sites.
Related Links	http://www.jbc.org/content/271/44/27730.abstract
Ending Page	27738
Starting Page	27730
Page Count	9
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	44
Volume Number	271
DOI	10.1074/jbc.271.44.27730
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1996-11-01
Access Restriction	Open
Subject Keyword	Enzymology
Alternative Title	ATP-dependent Degradation of CcdA by Lon Protease
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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