This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gottesman, S
Right arrow Articles by Maurizi, M R
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gottesman, S
Right arrow Articles by Maurizi, M R

 Previous Article  |  Next Article 

Microbiol Mol Biol Rev. 1992 December; 56(4): 592-621

Regulation by proteolysis: energy-dependent proteases and their targets.

S Gottesman and M R Maurizi

Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.

SUMMARY

A number of critical regulatory proteins in both prokaryotic and eukaryotic cells are subject to rapid, energy-dependent proteolysis. Rapid degradation combined with control over biosynthesis provides a mechanism by which the availability of a protein can be limited both temporally and spatially. Highly unstable regulatory proteins are involved in numerous biological functions, particularly at the commitment steps in developmental pathways and in emergency responses. The proteases involved in energy-dependent proteolysis are large proteins with the ability to use ATP to scan for appropriate targets and degrade complete proteins in a processive manner. These cytoplasmic proteases are also able to degrade many abnormal proteins in the cell.

Microbiol Mol Biol Rev. 1992 December; 56(4): 592-621




This article has been cited by other articles:

  • Narayanan, N., Chou, C. P. (2009). Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli. Appl. Environ. Microbiol. 75: 5424-5427 [Abstract] [Full Text]  
  • Andersson, F. I., Tryggvesson, A., Sharon, M., Diemand, A. V., Classen, M., Best, C., Schmidt, R., Schelin, J., Stanne, T. M., Bukau, B., Robinson, C. V., Witt, S., Mogk, A., Clarke, A. K. (2009). Structure and Function of a Novel Type of ATP-dependent Clp Protease. J. Biol. Chem. 284: 13519-13532 [Abstract] [Full Text]  
  • Weel-Sneve, R., Bjoras, M., Kristiansen, K. I. (2008). Overexpression of the LexA-regulated tisAB RNA in E. coli inhibits SOS functions; implications for regulation of the SOS response. Nucleic Acids Res 36: 6249-6259 [Abstract] [Full Text]  
  • Kario, E., Tirosh, B., Ploegh, H. L., Navon, A. (2008). N-Linked Glycosylation Does Not Impair Proteasomal Degradation but Affects Class I Major Histocompatibility Complex Presentation. J. Biol. Chem. 283: 244-254 [Abstract] [Full Text]  
  • Ganesan, B., Stuart, M. R., Weimer, B. C. (2007). Carbohydrate Starvation Causes a Metabolically Active but Nonculturable State in Lactococcus lactis. Appl. Environ. Microbiol. 73: 2498-2512 [Abstract] [Full Text]  
  • Michel, A., Agerer, F., Hauck, C. R., Herrmann, M., Ullrich, J., Hacker, J., Ohlsen, K. (2006). Global Regulatory Impact of ClpP Protease of Staphylococcus aureus on Regulons Involved in Virulence, Oxidative Stress Response, Autolysis, and DNA Repair.. J. Bacteriol. 188: 5783-5796 [Abstract] [Full Text]  
  • Madsen, M. L., Nettleton, D., Thacker, E. L., Edwards, R., Minion, F. C. (2006). Transcriptional Profiling of Mycoplasma hyopneumoniae during Heat Shock Using Microarrays. Infect. Immun. 74: 160-166 [Abstract] [Full Text]  
  • Buchler, N. E., Gerland, U., Hwa, T. (2005). Nonlinear protein degradation and the function of genetic circuits. Proc. Natl. Acad. Sci. USA 102: 9559-9564 [Abstract] [Full Text]  
  • Gribun, A., Kimber, M. S., Ching, R., Sprangers, R., Fiebig, K. M., 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 [Abstract] [Full Text]  
  • Suokko, A., Savijoki, K., Malinen, E., Palva, A., Varmanen, P. (2005). Characterization of a Mobile clpL Gene from Lactobacillus rhamnosus. Appl. Environ. Microbiol. 71: 2061-2069 [Abstract] [Full Text]  
  • Lee, A. Y.-L., Hsu, C.-H., Wu, S.-H. (2004). Functional Domains of Brevibacillus thermoruber Lon Protease for Oligomerization and DNA Binding: ROLE OF N-TERMINAL AND SENSOR AND SUBSTRATE DISCRIMINATION DOMAINS. J. Biol. Chem. 279: 34903-34912 [Abstract] [Full Text]  
  • Motaleb, M. A., Sal, M. S., Charon, N. W. (2004). The Decrease in FlaA Observed in a flaB Mutant of Borrelia burgdorferi Occurs Posttranscriptionally. J. Bacteriol. 186: 3703-3711 [Abstract] [Full Text]  
  • Liu, T., Lu, B., Lee, I., Ondrovicova, G., Kutejova, E., Suzuki, C. K. (2004). DNA and RNA Binding by the Mitochondrial Lon Protease Is Regulated by Nucleotide and Protein Substrate. J. Biol. Chem. 279: 13902-13910 [Abstract] [Full Text]  
  • Botos, I., Melnikov, E. E., Cherry, S., Tropea, J. E., Khalatova, A. G., Rasulova, F., Dauter, Z., Maurizi, M. R., Rotanova, T. V., Wlodawer, A., Gustchina, A. (2004). The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site. J. Biol. Chem. 279: 8140-8148 [Abstract] [Full Text]  
  • Kim, D. Y., Kim, K. K. (2003). Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori. J. Biol. Chem. 278: 50664-50670 [Abstract] [Full Text]  
  • Robertson, G. T., Ng, W.-L., Gilmour, R., Winkler, M. E. (2003). Essentiality of clpX, but Not clpP, clpL, clpC, or clpE, in Streptococcus pneumoniae R6. J. Bacteriol. 185: 2961-2966 [Abstract] [Full Text]  
  • Guo, F., Esser, L., Singh, S. K., Maurizi, M. R., Xia, D. (2002). Crystal Structure of the Heterodimeric Complex of the Adaptor, ClpS, with the N-domain of the AAA+ Chaperone, ClpA. J. Biol. Chem. 277: 46753-46762 [Abstract] [Full Text]  
  • Pratt, J. M., Petty, J., Riba-Garcia, I., Robertson, D. H. L., Gaskell, S. J., Oliver, S. G., Beynon, R. J. (2002). Dynamics of Protein Turnover, a Missing Dimension in Proteomics. Mol. Cell. Proteomics 1: 579-591 [Abstract] [Full Text]  
  • Seong, I. S., Kang, M. S., Choi, M. K., Lee, J. W., Koh, O. J., Wang, J., Eom, S. H., Chung, C. H. (2002). The C-terminal Tails of HslU ATPase Act as a Molecular Switch for Activation of HslV Peptidase. J. Biol. Chem. 277: 25976-25982 [Abstract] [Full Text]  
  • Robertson, G. T., Ng, W.-L., Foley, J., Gilmour, R., Winkler, M. E. (2002). Global Transcriptional Analysis of clpP Mutations of Type 2 Streptococcus pneumoniae and Their Effects on Physiology and Virulence. J. Bacteriol. 184: 3508-3520 [Abstract] [Full Text]  
  • Fukui, T., Eguchi, T., Atomi, H., Imanaka, T. (2002). A Membrane-Bound Archaeal Lon Protease Displays ATP-Independent Proteolytic Activity towards Unfolded Proteins and ATP-Dependent Activity for Folded Proteins. J. Bacteriol. 184: 3689-3698 [Abstract] [Full Text]  
  • Sobczyk, A., Bellier, A., Viala, J., Mazodier, P. (2002). The lon gene, encoding an ATP-dependent protease, is a novel member of the HAIR/HspR stress-response regulon in actinomycetes. Microbiology 148: 1931-1937 [Abstract] [Full Text]  
  • Kang, S. G., Ortega, J., Singh, S. K., Wang, N., Huang, N.-n., Steven, A. C., Maurizi, M. R. (2002). Functional Proteolytic Complexes of the Human Mitochondrial ATP-dependent Protease, hClpXP. J. Biol. Chem. 277: 21095-21102 [Abstract] [Full Text]  
  • Liu, S., Graham, J. E., Bigelow, L., Morse, P. D. II, Wilkinson, B. J. (2002). Identification of Listeria monocytogenes Genes Expressed in Response to Growth at Low Temperature. Appl. Environ. Microbiol. 68: 1697-1705 [Abstract] [Full Text]  
  • Pummi, T., Leskela, S., Wahlstrom, E., Gerth, U., Tjalsma, H., Hecker, M., Sarvas, M., Kontinen, V. P. (2002). ClpXP Protease Regulates the Signal Peptide Cleavage of Secretory Preproteins in Bacillus subtilis with a Mechanism Distinct from That of the Ecs ABC Transporter. J. Bacteriol. 184: 1010-1018 [Abstract] [Full Text]  
  • Lu, Z. H., Solioz, M. (2001). Copper-induced Proteolysis of the CopZ Copper Chaperone of Enterococcus hirae. J. Biol. Chem. 276: 47822-47827 [Abstract] [Full Text]  
  • Borezee, E., Pellegrini, E., Beretti, J.-L., Berche, P. (2001). SvpA, a novel surface virulence-associated protein required for intracellular survival of Listeria monocytogenes. Microbiology 147: 2913-2923 [Abstract] [Full Text]  
  • Klanner, C., Prokisch, H., Langer, T. (2001). MAP-1 and IAP-1, Two Novel AAA Proteases with Catalytic Sites on Opposite Membrane Surfaces in Mitochondrial Inner Membrane of Neurospora crassa. Mol. Biol. Cell 12: 2858-2869 [Abstract] [Full Text]  
  • Li, C., Tao, Y. P., Simon, L. D. (2000). Expression of Different-Size Transcripts from the clpP-clpX Operon of Escherichia coli during Carbon Deprivation. J. Bacteriol. 182: 6630-6637 [Abstract] [Full Text]  
  • Borezee, E., Msadek, T., Durant, L., Berche, P. (2000). Identification in Listeria monocytogenes of MecA, a Homologue of the Bacillus subtilis Competence Regulatory Protein. J. Bacteriol. 182: 5931-5934 [Abstract] [Full Text]  
  • Badger, J. L., Young, B. M., Darwin, A. J., Miller, V. L. (2000). Yersinia enterocolitica ClpB Affects Levels of Invasin and Motility. J. Bacteriol. 182: 5563-5571 [Abstract] [Full Text]  
  • Amerik, A. Y., Nowak, J., Swaminathan, S., Hochstrasser, M. (2000). The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways. Mol. Biol. Cell 11: 3365-3380 [Abstract] [Full Text]  
  • Whistler, C. A., Stockwell, V. O., Loper, J. E. (2000). Lon Protease Influences Antibiotic Production and UV Tolerance of Pseudomonas fluorescens Pf-5. Appl. Environ. Microbiol. 66: 2718-2725 [Abstract] [Full Text]  
  • Summers, M. L., Botero, L. M., Busse, S. C., McDermott, T. R. (2000). The Sinorhizobium meliloti Lon Protease Is Involved in Regulating Exopolysaccharide Synthesis and Is Required for Nodulation of Alfalfa. J. Bacteriol. 182: 2551-2558 [Abstract] [Full Text]  
  • Poteete, A. R., Fenton, A. C. (2000). Genetic Requirements of Phage lambda Red-Mediated Gene Replacement in Escherichia coli K-12. J. Bacteriol. 182: 2336-2340 [Abstract] [Full Text]  
  • Claret, L., Hughes, C. (2000). Rapid Turnover of FlhD and FlhC, the Flagellar Regulon Transcriptional Activator Proteins, during Proteus Swarming. J. Bacteriol. 182: 833-836 [Abstract] [Full Text]  
  • Suchland, R. J., Rockey, D. D., Bannantine, J. P., Stamm, W. E. (2000). Isolates of Chlamydia trachomatis That Occupy Nonfusogenic Inclusions Lack IncA, a Protein Localized to the Inclusion Membrane. Infect. Immun. 68: 360-367 [Abstract] [Full Text]  
  • Wickner, S., Maurizi, M. R., Gottesman, S. (1999). Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins. Science 286: 1888-1893 [Abstract] [Full Text]  
  • Qi, Z., Hamza, I., O'Brian, M. R. (1999). Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein. Proc. Natl. Acad. Sci. USA 96: 13056-13061 [Abstract] [Full Text]  
  • Wang, L., Wilson, S., Elliott, T. (1999). A Mutant HemA Protein with Positive Charge Close to the N Terminus Is Stabilized against Heme-Regulated Proteolysis in Salmonella typhimurium. J. Bacteriol. 181: 6033-6041 [Abstract] [Full Text]  
  • Johansson, J., Uhlin, B. E. (1999). Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli. Proc. Natl. Acad. Sci. USA 96: 10776-10781 [Abstract] [Full Text]  
  • Wickner, S., Maurizi, M. R. (1999). Here's the hook: Similar substrate binding sites in the chaperone domains of Clp and Lon. Proc. Natl. Acad. Sci. USA 96: 8318-8320 [Full Text]  
  • Spetea, C., Hundal, T., Lohmann, F., Andersson, B. (1999). GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein. Proc. Natl. Acad. Sci. USA 96: 6547-6552 [Abstract] [Full Text]  
  • Ebel, W., Skinner, M. M., Dierksen, K. P., Scott, J. M., Trempy, J. E. (1999). A Conserved Domain in Escherichia coli Lon Protease Is Involved in Substrate Discriminator Activity. J. Bacteriol. 181: 2236-2243 [Abstract] [Full Text]  
  • Kallio, P. J., Wilson, W. J., O'Brien, S., Makino, Y., Poellinger, L. (1999). Regulation of the Hypoxia-inducible Transcription Factor 1alpha by the Ubiquitin-Proteasome Pathway. J. Biol. Chem. 274: 6519-6525 [Abstract] [Full Text]  
  • Wang, L., Elliott, M., Elliott, T. (1999). Conditional Stability of the HemA Protein (Glutamyl-tRNA Reductase) Regulates Heme Biosynthesis in Salmonella typhimurium. J. Bacteriol. 181: 1211-1219 [Abstract] [Full Text]  
  • Cha, H. J., Srivastava, R., Vakharia, V. N., Rao, G., Bentley, W. E. (1999). Green Fluorescent Protein as a Noninvasive Stress Probe in Resting Escherichia coli Cells. Appl. Environ. Microbiol. 65: 409-414 [Abstract] [Full Text]  
  • Li, X., Zhao, X., Fang, Y., Jiang, X., Duong, T., Fan, C., Huang, C.-C., Kain, S. R. (1998). Generation of Destabilized Green Fluorescent Protein as a Transcription Reporter. J. Biol. Chem. 273: 34970-34975 [Abstract] [Full Text]  
  • Yoo, S. J., Kim, H. H., Shin, D. H., Lee, C. S., Seong, I. S., Seol, J. H., Shimbara, N., Tanaka, K., Chung, C. H. (1998). 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. 273: 22929-22935 [Abstract] [Full Text]  
  • Rao, M. B., Tanksale, A. M., Ghatge, M. S., Deshpande, V. V. (1998). Molecular and Biotechnological Aspects of Microbial Proteases. Microbiol. Mol. Biol. Rev. 62: 597-635 [Abstract] [Full Text]  
  • van Dijl, J. M., Kutejova, E., Suda, K., Schatz, G., Suzuki, C. K. (1998). The ATPase and protease domains of yeast mitochondrial Lon: Roles in proteolysis and respiration-dependent growth. Proc. Natl. Acad. Sci. USA 95: 10584-10589 [Abstract] [Full Text]  
  • Hamza, I., Chauhan, S., Hassett, R., O'Brian, M. R. (1998). The Bacterial Irr Protein Is Required for Coordination of Heme Biosynthesis with Iron Availability. J. Biol. Chem. 273: 21669-21674 [Abstract] [Full Text]  
  • Arkin, A., Ross, J., McAdams, H. H. (1998). Stochastic Kinetic Analysis of Developmental Pathway Bifurcation in Phage {lambda}-Infected Escherichia coli Cells. Genetics 149: 1633-1648 [Abstract] [Full Text]  
  • Grimaud, R., Kessel, M., Beuron, F., Steven, A. C., Maurizi, M. R. (1998). Enzymatic and Structural Similarities between the Escherichia coli ATP-dependent Proteases, ClpXP and ClpAP. J. Biol. Chem. 273: 12476-12481 [Abstract] [Full Text]  
  • van Dyck, L., Neupert, W., Langer, T. (1998). The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondria. Genes Dev. 12: 1515-1524 [Abstract] [Full Text]  
  • Kelly, A. J., Sackett, M. J., Din, N., Quardokus, E., Brun, Y. V. (1998). Cell cycle-dependent transcriptional and proteolytic regulation of FtsZ in Caulobacter. Genes Dev. 12: 880-893 [Abstract] [Full Text]  
  • Jones, J. M., Welty, D. J., Nakai, H. (1998). Versatile Action of Escherichia coli ClpXP as Protease or Molecular Chaperone for Bacteriophage Mu Transposition. J. Biol. Chem. 273: 459-465 [Abstract] [Full Text]  
  • Hilliard, J. J., Maurizi, M. R., Simon, L. D. (1998). Isolation and Characterization of the Phage T4 PinA Protein, an Inhibitor of the ATP-dependent Lon Protease of Escherichia coli. J. Biol. Chem. 273: 518-523 [Abstract] [Full Text]  
  • Pearce, D. A., Sherman, F. (1997). Differential Ubiquitin-dependent Degradation of the Yeast Apo-cytochrome c Isozymes. J. Biol. Chem. 272: 31829-31836 [Abstract] [Full Text]  
  • Popham, P. L., Hahn, T.-W., Krebes, K. A., Krause, D. C. (1997). Loss of HMW1 and HMW3 in noncytadhering mutants of Mycoplasma pneumoniae occurs post-translationally. Proc. Natl. Acad. Sci. USA 94: 13979-13984 [Abstract] [Full Text]  
  • Harris, R. S., Feng, G., Ross, K. J., Sidhu, R., Thulin, C., Longerich, S., Szigety, S. K., Winkler, M. E., Rosenberg, S. M. (1997). Mismatch repair protein MutL becomes limiting during stationary-phase mutation. Genes Dev. 11: 2426-2437 [Abstract] [Full Text]  
  • Huang, H.-C., Goldberg, A. L. (1997). Proteolytic Activity of the ATP-dependent Protease HslVU Can Be Uncoupled from ATP Hydrolysis. J. Biol. Chem. 272: 21364-21372 [Abstract] [Full Text]  
  • Levchenko, I, Yamauchi, M, Baker, T A (1997). ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway.. Genes Dev. 11: 1561-1572 [Abstract]  
  • Kihara, A., Akiyama, Y., Ito, K. (1997). Host regulation of lysogenic decision in bacteriophage lambda : Transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA). Proc. Natl. Acad. Sci. USA 94: 5544-5549 [Abstract] [Full Text]  
  • Skorko-Glonek, J., Skórko-Glonek, J., Krzewski, K., Zolese, G., Bertoli, E., Tanfani, F. (1997). HtrA Heat Shock Protease Interacts with Phospholipid Membranes and Undergoes Conformational Changes. J. Biol. Chem. 272: 8974-8982 [Abstract] [Full Text]  
  • Bercovich, B., Stancovski, I., Mayer, A., Blumenfeld, N., Laszlo, A., Schwartz, A. L., Ciechanover, A. (1997). Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70. J. Biol. Chem. 272: 9002-9010 [Abstract] [Full Text]  
  • Gottesman, S, Wickner, S, Maurizi, M R (1997). Protein quality control: triage by chaperones and proteases.. Genes Dev. 11: 815-823  
  • Jubete, Y., Maurizi, M. R., Gottesman, S. (1996). Role of the Heat Shock Protein DnaJ in the Lon-dependent Degradation of Naturally Unstable Proteins. J. Biol. Chem. 271: 30798-30803 [Abstract] [Full Text]  
  • Lindahl, M., Tabak, S., Cseke, L., Pichersky, E., Andersson, B., Adam, Z. (1996). Identification, Characterization, and Molecular Cloning of a Homologue of the Bacterial FtsH Protease in Chloroplasts of Higher Plants. J. Biol. Chem. 271: 29329-29334 [Abstract] [Full Text]  
  • Van Melderen, L., Thi, M. H. D., Lecchi, P., Gottesman, S., Couturier, M., Maurizi, M. R. (1996). ATP-dependent Degradation of CcdA by Lon Protease. EFFECTS OF SECONDARY STRUCTURE AND HETEROLOGOUS SUBUNIT INTERACTIONS. J. Biol. Chem. 271: 27730-27738 [Abstract] [Full Text]  
  • Wright, R, Stephens, C, Zweiger, G, Shapiro, L, Alley, M R (1996). Caulobacter Lon protease has a critical role in cell-cycle control of DNA methylation.. Genes Dev. 10: 1532-1542 [Abstract]  
  • Yoo, S. J., Seol, J. H., Shin, D. H., Rohrwild, M., Kang, M.-S., Tanaka, K., Goldberg, A. L., Chung, C. H. (1996). Purification and Characterization of the Heat Shock Proteins HslV and HslU That Form a New ATP-dependent Protease in Escherichia coli. J. Biol. Chem. 271: 14035-14040 [Abstract] [Full Text]  
  • Teichmann, U., van Dyck, L., Guiard, B., Fischer, H., Glockshuber, R., Neupert, W., Langer, T. (1996). Substitution of PIM1 Protease in Mitochondria by Escherichia coli Lon Protease. J. Biol. Chem. 271: 10137-10142 [Abstract] [Full Text]  
  • Scholze, H., Frey, S., Cejka, Z., Bakker-Grunwald, T. (1996). Evidence for the Existence of both Proteasomes and a Novel High Molecular Weight Peptidase in Entamoeba histolytica. J. Biol. Chem. 271: 6212-6216 [Abstract] [Full Text]  
  • Li, X., Stebbins, B., Hoffman, L., Pratt, G., Rechsteiner, M., Coffino, P. (1996). The N Terminus of Antizyme Promotes Degradation of Heterologous Proteins. J. Biol. Chem. 271: 4441-4446 [Abstract] [Full Text]  
  • Li, X., Coffino, P. (1996). Identification of a Region of p53 That Confers Lability. J. Biol. Chem. 271: 4447-4451 [Abstract] [Full Text]  
  • Keiler, K. C., Sauer, R. T. (1996). Sequence Determinants of C-terminal Substrate Recognition by the Tsp Protease. J. Biol. Chem. 271: 2589-2593 [Abstract] [Full Text]  
  • Kim, K. I., Baek, S. H., Hong, Y.-M., Kang, M.-S., Ha, D. B., Goldberg, A. L., Chung, C. H. (1995). Purification and Characterization of Protease Ci, a Cytoplasmic Metalloendoprotease in Escherichia coli. J. Biol. Chem. 270: 29799-29805 [Abstract] [Full Text]  
  • Schork, S. M., Thumm, M., Wolf, D. H. (1995). Catabolite Inactivation of Fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. J. Biol. Chem. 270: 26446-26450 [Abstract] [Full Text]  
  • Li, H. H., Merchant, S. (1995). Degradation of Plastocyanin in Copper-deficient Chlamydomonas reinhardtii. J. Biol. Chem. 270: 23504-23510 [Abstract] [Full Text]  
  • Levchenko, I, Luo, L, Baker, T A (1995). Disassembly of the Mu transposase tetramer by the ClpX chaperone.. Genes Dev. 9: 2399-2408 [Abstract]  
  • Seol, J. H., Baek, S. H., Kang, M.-S., Ha, D. B., 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 [Abstract] [Full Text]  
  • Varshavsky, A. (1995). The N-end Rule. Cold Spring Harb Symp Quant Biol 60: 461-478 [Abstract]  
  • Hochstrasser, M., Papa, F.R., Chen, P., Swaminathan, S., Johnson, P., Stillman, L., Amerik, A.Y., Li, S.-J. (1995). The DOA Pathway: Studies on the Functions and Mechanisms of Ubiquitin-dependent Protein Degradation in the Yeast Saccharomyces cerevisiae. Cold Spring Harb Symp Quant Biol 60: 503-513 [Abstract]  
  • Chung, C. (1993). Proteases in Escherichia coli. Science 262: 372-374  
  • Huang, H.-C., Sherman, M. Y., Kandror, O., Goldberg, A. L. (2001). The Molecular Chaperone DnaJ Is Required for the Degradation of a Soluble Abnormal Protein in Escherichia coli. J. Biol. Chem. 276: 3920-3928 [Abstract] [Full Text]  
  • Barnett, M. E., Zolkiewska, A., Zolkiewski, M. (2000). Structure and Activity of ClpB from Escherichia coli. ROLE OF THE AMINO- AND CARBOXYL-TERMINAL DOMAINS. J. Biol. Chem. 275: 37565-37571 [Abstract] [Full Text]  
  • Singh, S. K., Rozycki, J., Ortega, J., Ishikawa, T., Lo, J., Steven, A. C., Maurizi, M. R. (2001). Functional Domains of the ClpA and ClpX Molecular Chaperones Identified by Limited Proteolysis and Deletion Analysis. J. Biol. Chem. 276: 29420-29429 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»