ClpS modulates but is not essential for bacterial N-end rule degradation

Genes and Development

Volumn 21, Issue 4, 2007, Pages 403-408

  Wang, Kevin H ^a   Sauer, Robert T ^a   Baker, Tania A ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Degradation motif; PheS; SUMO; Targeted proteolysis

Indexed keywords

ADAPTOR PROTEIN; PROTEIN CLPS; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIUM; BIOASSAY; CONTROLLED STUDY; GENETIC SCREENING; IN VIVO STUDY; MODULATION; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN METABOLISM;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARRIER PROTEINS; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEINS; MOLECULAR SEQUENCE DATA; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS);

EID: 33847226240     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.1511907     Document Type: Article

References (25)

1. Bachmair, A., Finley, D., and Varshavsky, A. 1986. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179-186.
2. Benaroudj, N., Tarcsa, E., Cascio, P., and Goldberg, A.L. 2001. The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes. Biochimie 83: 311-318.
3. Craig, K.L. and Tyers, M. 1999. The F-box: A new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction. Prog. Biophys. Mol. Biol. 72: 299-328.
4. Dougan, D.A., Reid, B.G., Horwich, A.L., and Bukau, B. 2002. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 9: 673-683.
5. Erbse, A., Schmidt, R., Bornemann, T., Schneider-Mergener, J., Mogk, A., Zahn, R., Dougan, D.A., and Bukau, B. 2006. ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature 439: 753-756.
6. Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30: 465-506.
7. Gottesman, S., Roche, E., Zhou, Y., and Sauer, R.T. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes & Dev. 12: 1338-1347.
8. Kast, P. 1994. pKSS - A second-generation general purpose cloning vector for efficient positive selection of recombinant clones. Gene 138: 109-114.
9. Kast, P. and Hennecke, H. 1991. Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations. J. Mol. Biol. 222: 99-124.
10. 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.
11. Kenniston, J.A., Baker, T.A., Fernandez, J.M., and Sauer, R.T. 2003. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114: 511-520.
12. Kim, Y.I., Burton, R.E., Burton, B.M., Sauer, R.T., and Baker, T.A. 2000. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell 5: 639-648.
13. Li, S.J. and Hochstrasser, M. 1999. A new protease required for cell-cycle progression in yeast. Nature 398: 246-251.
14. Levchenko, I., Seidel, M., Sauer, R.T., and Baker, T.A. 2000. A specificity-enhancing factor for the ClpXP degradation machine. Science 289: 2354-2356.
15. Malakhov, M.P., Mattern, M.R., Malakhova, O.A., Drinker, M., Weeks, S.D., and Butt, T.R. 2004. SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins. J. Struct. Funct. Genomics 5: 75-86.
16. Maurizi, M.R., Clark, W.P., Katayama, Y., Rudikoff, S., Pumphrey, J., Bowers, B., and Gottesman, S. 1990. Sequence and structure of ClpP, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 265: 12536-12545.
17. Parsell, D., Silber, K.R., and Sauer, R.T. 1990. Carboxy-terminal determinants of intracellular protein degradation. Genes & Dev. 4: 277-286.
18. Pickart, C.M. 1997. Targeting of substrates to the 26S proteasome. FASEB J. 11: 1055-1066.
19. Reidhaar-Olson, J.F., Bowie, J.U., Breyer, R.M., Hu, J.C., Knight, K.L., Lim, W.A., Mossing, M.C., Parsell, D.A., Shoemaker, K.R., and Sauer, R.T. 1991. Random mutagenesis of protein sequences using oligonucleotide cassettes. Methods Enzymol. 208: 564-586.
20. Schirmer, E.C., Glover, J.R., Singer, M.A., and Lindquist, S. 1996. HSP100/Clp proteins: A common mechanism explains diverse functions. Trends Biochem. Sci. 21: 289-296.
21. Singh, S.K., Grimaud, R., Hoskins, J.R., Wickner, S., and Maurizi, M.R. 2000. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. Proc. Natl. Acad. Sci. 97: 8898-8903.
22. Tobias, J.W., Shrader, T.E., Rocap, G., and Varshavsky, A. 1991. The N-end rule in bacteria. Science 254: 1374-1377.
23. Varshavsky, A. 1992. The N-end rule. Cell 69: 725-735.
24. 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.
25. Xia, D., Esser, L., Singh, S.K., Guo, F., and Maurizi, M.R. 2004. Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone. J. Struct. Biol. 146: 166-179.