Assembly pathway of an AAA+ protein: Tracking ClpA and ClpAP complex formation in real time

Biochemistry

Volumn 46, Issue 21, 2007, Pages 6183-6193

  Kress, Wolfgang ^a   Mutschler, Hannes ^a   Weber Ban, Eilika ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; DEGRADATION; FLUORESCENCE; KINETICS; NUMERICAL METHODS; OLIGOMERS; REAL TIME CONTROL;

BACTERIAL CHAPERONES; HEXAMERIZATION; HEXAMERS; RATE PARAMETERS;

PROTEINS;

CHAPERONE; PROTEIN DERIVATIVE; PROTEINASE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME KINETICS; KINETICS; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEINS; KINETICS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MULTIPROTEIN COMPLEXES; PROTEIN BINDING; PROTEIN CONFORMATION;

BACTERIA (MICROORGANISMS);

EID: 34249734248     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602616t     Document Type: Article

References (25)

1. Lupas, A., Flanagan, J. M., Tamura, T., and Baumeister, W. (1997) Self-compartmentalizing proteases, Trends Biochem. Sci. 22, 399-404.
2. Suzuki, C. K., Rep, M., van Dijl, J. M., Suda, K., Grivell, L. A., and Schatz, G. (1997) ATP-dependent proteases that also chaperone protein biogenesis, Trends Biochem. Sci. 22, 118-123.
3. Gottesman, S. (1996) Proteases and their targets in Escherichia coli, Annu. Rev. Genet. 30, 465-506.
4. Sauer, R. T., Bolon, D. N., Burton, B. M., Burton, R. E., Flynn, J. M., Grant, R. A., Hersch, G. L., Joshi, S. A., Kenniston, J. A., Levchenko, I., Neher, S. B., Oakes, E. S., Siddiqui, S. M., Wah, D. A., and Baker, T. A. (2004) Sculpting the proteome with AAA(+) proteases and disassembly machines, Cell 119, 9-18.
5. Hwang, B. J., Woo, K. M., Goldberg, A. L., and Chung, C. H. (1988) Protease Ti, a new ATP-dependent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits, J. Biol. Chem. 263, 8727-8734.
6. Katayama-Fujimura, Y., Gottesman, S., and Maurizi, M. R. (1987) A multiple-component, ATP-dependent protease from Escherichia coli, J. Biol. Chem. 262, 4477-4485.
7. Katayama, Y., Gottesman, S., Pumphrey, J., Rudikoff, S., Clark, W. P., and Maurizi, M. R. (1988) The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component, J. Biol. Chem. 263, 15226-15236.
8. Wang, J., Hartling, J. A., and Flanagan, J. M. (1997) The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis, Cell 91, 447-456.
9. Kessel, M., Maurizi, M. R., Kim, B., Kocsis, E., Trus, B. L., Singh, S. K., and Steven, A. C. (1995) Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome, J. Mol. Biol. 250, 587-594.
10. Maurizi, M. R., Singh, S. K., Thompson, M. W., Kessel, M., and Ginsburg, A. (1998) Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP, Biochemistry 37, 7778-7786.
11. Woo, K. M., Chung, W. J., Ha, D. B., Goldberg, A. L., and Chung, C. H. (1989) Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides, J. Biol. Chem. 264, 2088-2091.
12. Weber-Ban, E. U., Reid, B. G., Miranker, A. D., and Horwich, A. L. (1999) Global unfolding of a substrate protein by the Hsp100 chaperone ClpA, Nature 401, 90-93.
13. Reid, B. G., Fenton, W. A., Horwich, A. L., and Weber-Ban, E. U. (2001) ClpA mediates directional translocation of substrate proteins into the ClpP protease, Proc. Natl. Acad. Sci. U.S.A. 98, 3768-3772.
14. Singh, S. K., Guo, F., and Maurizi, M. R. (1999) ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease, Biochemistry 38, 14906-14915.
15. Guo, F., Maurizi, M. R., Esser, L., and Xia, D. (2002) Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease, J. Biol. Chem. 277, 46743-46752.
16. Seol, J. H., Baek, S. H., Kang, M. S., Ha, D. B., and Chung, C. H. (1995) Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli, J. Biol. Chem. 270, 8087-8092.
17. Singh, S. K., and Maurizi, M. R. (1994) Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli, J. Biol. Chem. 269, 29537-29545.
18. Rieger, C. E., Lee, J., and Turnbull, J. L. (1997) A continuous spectrophotometric assay for aspartate transcarbamylase and ATPases, Anal. Biochem. 246, 86-95.
19. Gribun, A., Kimber, M. S., Ching, R., Sprangers, R., Fiebig, K. M., and Houry, W. A. (2005) The ClpP double-ring tetradecameric protease exhibits plastic ring-ring interactions, and the N-termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation, J. Biol. Chem. 280, 16185-16196.
20. Rouiller, I., Butel, V. M., Latterich, M., Milligan, R. A., and Wilson-Kubalek, E. M. (2000) A major conformational change in p97 AAA ATPase upon ATP binding, Mol. Cell 6, 1485-1490.
21. Monod, J., Wyman, J., and Changeux, J. P. (1965) On the Nature of Allosteric Transitions: A Plausible Model, J. Mol. Biol. 12, 88-118.
22. Bewley, M. C., Graziano, V., Griffin, K., and Flanagan, J. M. (2006) The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes, J. Struct. Biol. 153, 113-128.
23. Farrell, C. M., Grossman, A. D., and Sauer, R. T. (2005) Cytoplasmic degradation of ssrA-tagged proteins, Mol. Microbiol. 57, 1750-1761.
24. Turgay, K., Persuh, M., Hahn, J., and Dubnau, D. (2001) Roles of the two ClpC ATP binding sites in the regulation of competence and the stress response, Mol. Microbiol. 42, 717-727.
25. Kirstein, J., Schlothauer, T., Dougan, D. A., Lilie, H., Tischendorf, G., Mogk, A., Bukau, B., and Turgay, K. (2006) Adaptor protein controlled oligomerization activates the AAA+ protein ClpC, EMBO J. 25, 1481-1491.