| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
(Received for publication, July 10, 1996)
From the 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
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27730-27738
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
EFFECTS OF SECONDARY STRUCTURE AND HETEROLOGOUS SUBUNIT
INTERACTIONS
,
,
and
Laboratoire de Genetique, Departement de
Biologie Moleculaire, Universite Libre de Bruxelles, rue des Chevaux,
67, B-1640 Rhode Saint Genese, Belgium, the Laboratories of '' Cell
Biology and 
Molecular Biology, National Cancer Institute,
Bethesda, Maryland 20892, § Dienst Ultrastruktuur,
Institut Moleculaire Biologie, Vrije Universiteit Brussel,
Paardenstraat 65, B-1640 Rhode Saint Genese, Belgium, and the
¶ Laboratory of Analytical Chemistry, NIDDK, National Institutes
of Health, Bethesda, Maryland 20892
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 
-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 -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.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Raghava, B. Barua, P. K. Singh, M. Das, L. Madan, S. Bhattacharyya, K. Bajaj, B. Gopal, R. Varadarajan, and M. N. Gupta Refolding and simultaneous purification by three-phase partitioning of recombinant proteins from inclusion bodies Protein Sci., November 1, 2008; 17(11): 1987 - 1997. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Takaya, F. Tabuchi, H. Tsuchiya, E. Isogai, and T. Yamamoto Negative Regulation of Quorum-Sensing Systems in Pseudomonas aeruginosa by ATP-Dependent Lon Protease J. Bacteriol., June 15, 2008; 190(12): 4181 - 4188. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Oberer, K. Zangger, K. Gruber, and W. Keller The solution structure of ParD, the antidote of the ParDE toxin antitoxin module, provides the structural basis for DNA and toxin binding Protein Sci., August 1, 2007; 16(8): 1676 - 1688. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Wilbaux, N. Mine, A.-M. Guerout, D. Mazel, and L. Van Melderen Functional Interactions between Coexisting Toxin-Antitoxin Systems of the ccd Family in Escherichia coli O157:H7 J. Bacteriol., April 1, 2007; 189(7): 2712 - 2719. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. B. Smith and A. Maxwell A strand-passage conformation of DNA gyrase is required to allow the bacterial toxin, CcdB, to access its binding site Nucleic Acids Res., October 18, 2006; 34(17): 4667 - 4676. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. Cherny, L. Rockah, and E. Gazit The YoeB Toxin Is a Folded Protein That Forms a Physical Complex with the Unfolded YefM Antitoxin: IMPLICATIONS FOR A STRUCTURAL-BASED DIFFERENTIAL STABILITY OF TOXIN-ANTITOXIN SYSTEMS J. Biol. Chem., August 26, 2005; 280(34): 30063 - 30072. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Lah, M. Simic, G. Vesnaver, I. Marianovsky, G. Glaser, H. Engelberg-Kulka, and R. Loris Energetics of Structural Transitions of the Addiction Antitoxin MazE: IS A PROGRAMMED BACTERIAL CELL DEATH DEPENDENT ON THE INTRINSICALLY FLEXIBLE NATURE OF THE ANTITOXINS? J. Biol. Chem., April 29, 2005; 280(17): 17397 - 17407. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Liu, B. Lu, I. Lee, G. Ondrovicova, E. Kutejova, and C. K. Suzuki DNA and RNA Binding by the Mitochondrial Lon Protease Is Regulated by Nucleotide and Protein Substrate J. Biol. Chem., April 2, 2004; 279(14): 13902 - 13910. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. A. Defenbaugh and H. Nakai A Context-dependent ClpX Recognition Determinant Located at the C Terminus of Phage Mu Repressor J. Biol. Chem., December 26, 2003; 278(52): 52333 - 52339. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Loris, I. Marianovsky, J. Lah, T. Laeremans, H. Engelberg-Kulka, G. Glaser, S. Muyldermans, and L. Wyns Crystal Structure of the Intrinsically Flexible Addiction Antidote MazE J. Biol. Chem., July 18, 2003; 278(30): 28252 - 28257. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Fukui, T. Eguchi, H. Atomi, and T. Imanaka A Membrane-Bound Archaeal Lon Protease Displays ATP-Independent Proteolytic Activity towards Unfolded Proteins and ATP-Dependent Activity for Folded Proteins J. Bacteriol., July 1, 2002; 184(13): 3689 - 3698. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Allali, H. Afif, M. Couturier, and L. Van Melderen The Highly Conserved TldD and TldE Proteins of Escherichia coli Are Involved in Microcin B17 Processing and in CcdA Degradation J. Bacteriol., June 15, 2002; 184(12): 3224 - 3231. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. Narberhaus {alpha}-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network Microbiol. Mol. Biol. Rev., March 1, 2002; 66(1): 64 - 93. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M.-H. Dao-Thi, D. Charlier, R. Loris, D. Maes, J. Messens, L. Wyns, and J. Backmann Intricate Interactions within the ccd Plasmid Addiction System J. Biol. Chem., January 25, 2002; 277(5): 3733 - 3742. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Gerdes Toxin-Antitoxin Modules May Regulate Synthesis of Macromolecules during Nutritional Stress J. Bacteriol., February 1, 2000; 182(3): 561 - 572. [Full Text]
|
|
|
|
 |
|
 S. Wickner and M. R. Maurizi Here's the hook: Similar substrate binding sites in the chaperone domains of Clp and Lon PNAS, July 20, 1999; 96(15): 8318 - 8320. [Full Text] [PDF]
|
|
|
|
|
|
E. Gazit and R. T. Sauer The Doc Toxin and Phd Antidote Proteins of the Bacteriophage P1 Plasmid Addiction System Form a Heterotrimeric Complex J. Biol. Chem., June 11, 1999; 274(24): 16813 - 16818. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Stahlberg, E. Kutejova, K. Suda, B. Wolpensinger, A. Lustig, G. Schatz, A. Engel, and C. K. Suzuki Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits PNAS, June 8, 1999; 96(12): 6787 - 6790. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Van Melderen and S. Gottesman Substrate sequestration by a proteolytically inactive Lon mutant PNAS, May 25, 1999; 96(11): 6064 - 6071. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. M. Bahassi, M. H. O'Dea, N. Allali, J. Messens, M. Gellert, and M. Couturier Interactions of CcdB with DNA Gyrase. INACTIVATION OF GyrA, POISONING OF THE GYRASE-DNA COMPLEX, AND THE ANTIDOTE ACTION OF CcdA J. Biol. Chem., April 16, 1999; 274(16): 10936 - 10944. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Gonzalez, E. G. Frank, A. S. Levine, and R. Woodgate Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis Genes & Dev., December 15, 1998; 12(24): 3889 - 3899. [Abstract] [Full Text]
|
|
|
|
|
|
S. J. Yoo, H. H. Kim, D. H. Shin, C. S. Lee, I. S. Seong, J. H. Seol, N. Shimbara, K. Tanaka, and C. H. Chung Effects of the Cys Mutations on Structure and Function of the ATP-dependent HslVU Protease in Escherichia coli. THE CYS287 TO VAL MUTATION IN HslU UNCOUPLES THE ATP-DEPENDENT PROTEOLYSIS BY HslVU FROM ATP HYDROLYSIS J. Biol. Chem., September 4, 1998; 273(36): 22929 - 22935. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. B. Rao, A. M. Tanksale, M. S. Ghatge, and V. V. Deshpande Molecular and Biotechnological Aspects of Microbial Proteases Microbiol. Mol. Biol. Rev., September 1, 1998; 62(3): 597 - 635. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Sarria, A. Lyznik, C. E. Vallejos, and S. A. Mackenzie A Cytoplasmic Male Sterility–Associated Mitochondrial Peptide in Common Bean Is Post-Translationally Regulated PLANT CELL, July 1, 1998; 10(7): 1217 - 1228. [Abstract] [Full Text]
|
|
|
|
|
|
J. J. Hilliard, L. D. Simon, L. Van Melderen, and M. R. Maurizi PinA Inhibits ATP Hydrolysis and Energy-dependent Protein Degradation by Lon Protease J. Biol. Chem., January 2, 1998; 273(1): 524 - 527. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H.-C. Huang and A. L. Goldberg Proteolytic Activity of the ATP-dependent Protease HslVU Can Be Uncoupled from ATP Hydrolysis J. Biol. Chem., August 22, 1997; 272(34): 21364 - 21372. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S Gottesman, S Wickner, and M R Maurizi Protein quality control: triage by chaperones and proteases. Genes & Dev., April 1, 1997; 11(7): 815 - 823. [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
