Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*
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Ji-Joon Song | Ji-Joon Song | S. Eom | Jimin Wang | J. Seol | C. Chung | I. Seong | Jimin Wang | O. Bang | Jae Hong Seol | Soo Hyun Eom | E. Park | Chin Ha Chung | Ihn Sik Seong | Eunyong Park | Oksun Bang | Young Min Rho | Ohn-Jo Koh | Sung Won Ahn | O. Koh
[1] T. Baker,et al. Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. , 2004, Genes & development.
[2] J. Wang,et al. Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU. , 2001, Structure.
[3] Bernd Bukau,et al. Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB , 2004, Cell.
[4] J. Seol,et al. ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli. , 1997, Biochemical and biophysical research communications.
[5] M. M. Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.
[6] D. A. Dougherty,et al. Cation-π interactions in structural biology , 1999 .
[7] M. Zółkiewski,et al. ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein Aggregation , 1999, The Journal of Biological Chemistry.
[8] Christopher A. Hunter,et al. The nature of .pi.-.pi. interactions , 1990 .
[9] T. Langer,et al. AAA proteases: cellular machines for degrading membrane proteins. , 2000, Trends in biochemical sciences.
[10] S. Rüdiger,et al. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB , 1999, The EMBO journal.
[11] W. Baumeister,et al. The 26S proteasome: a molecular machine designed for controlled proteolysis. , 1999, Annual review of biochemistry.
[12] D. Mckay,et al. Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning. , 2001, Acta crystallographica. Section D, Biological crystallography.
[13] A. Wilkinson,et al. AAA+ superfamily ATPases: common structure–diverse function , 2001, Genes to cells : devoted to molecular & cellular mechanisms.
[14] M. Yohda,et al. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[15] A. Goldberg,et al. HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[16] Y. Ishii,et al. Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon , 1997, Molecular and General Genetics MGG.
[17] D. Parry,et al. Secondary structure of bovine ?- and ?-casein in solution , 1981 .
[18] J. Seol,et al. Mutagenesis of two N‐terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP‐dependent HslVU protease , 1997, FEBS letters.
[19] S. Gottesman,et al. Proteases and their targets in Escherichia coli. , 1996, Annual review of genetics.
[20] Keiji Tanaka,et al. The ATP‐dependent CodWX (HslVU) protease in Bacillus subtilis is an N‐terminal serine protease , 2001, The EMBO journal.
[21] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[22] J. Wang,et al. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. , 2001, Structure.
[23] A. Goldberg,et al. Purification and Characterization of the Heat Shock Proteins HslV and HslU That Form a New ATP-dependent Protease in Escherichia coli* , 1996, The Journal of Biological Chemistry.
[24] K. Tanaka,et al. The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli , 2000, FEBS letters.
[25] Robert E. Cohen,et al. Proteasomes and their kin: proteases in the machine age , 2004, Nature Reviews Molecular Cell Biology.
[26] A. Goldberg. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. , 1992, European journal of biochemistry.
[27] M. Webb. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[28] A. Matouschek. Protein unfolding--an important process in vivo? , 2003, Current opinion in structural biology.
[29] G. Petsko,et al. Weakly polar interactions in proteins. , 1988, Advances in protein chemistry.
[30] M. Khattar. Overexpression of the hslVU operon suppresses SOS‐mediated inhibition of cell division in Escherichia coli , 1997, FEBS letters.
[31] Christine B. Trame,et al. Crystal and Solution Structures of an HslUV Protease–Chaperone Complex , 2000, Cell.
[32] S. Gottesman,et al. Proteolysis in bacterial regulatory circuits. , 2003, Annual review of cell and developmental biology.
[33] R. Gayda,et al. Regulation of cell division in Escherichia coli: SOS induction and cellular location of the sulA protein, a key to lon-associated filamentation and death , 1984, Journal of bacteriology.
[34] C. Gross,et al. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. , 2003, Molecular cell.
[35] E. Bi,et al. Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring , 1993, Journal of bacteriology.
[36] R. Huber,et al. Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY) , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[37] D. A. Dougherty,et al. Cation-π Interactions in Chemistry and Biology: A New View of Benzene, Phe, Tyr, and Trp , 1996, Science.
[38] J. Tkach,et al. Evidence for an Unfolding/Threading Mechanism for Protein Disaggregation by Saccharomyces cerevisiae Hsp104* , 2004, Journal of Biological Chemistry.
[39] Wolfgang Baumeister,et al. The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome , 1997, Nature Structural Biology.
[40] S. Gottesman,et al. Protein degradation in Escherichia coli: the lon gene controls the stability of sulA protein. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[41] A. Matouschek,et al. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. , 2001, Molecular cell.
[42] J M Thornton,et al. Pi-pi interactions: the geometry and energetics of phenylalanine-phenylalanine interactions in proteins. , 1991, Journal of molecular biology.
[43] S. Eom,et al. The C-terminal Tails of HslU ATPase Act as a Molecular Switch for Activation of HslV Peptidase* , 2002, The Journal of Biological Chemistry.
[44] D. Mckay,et al. Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome. , 2003, Journal of molecular biology.
[45] P. Schultz,et al. Substrate recognition by the AAA+ chaperone ClpB , 2004, Nature Structural &Molecular Biology.
[46] Robert Huber,et al. The structures of HslU and the ATP-dependent protease HslU–HslV , 2000, Nature.
[47] J. Seol,et al. ATP‐dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli , 1999, FEBS letters.
[48] R. Huber,et al. Crystal structure of heat shock locus V (HslV) from Escherichia coli. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[49] A. Goldberg,et al. The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase. , 1997, European journal of biochemistry.
[50] T. Ogura,et al. Conserved Pore Residues in the AAA Protease FtsH Are Important for Proteolysis and Its Coupling to ATP Hydrolysis* , 2003, Journal of Biological Chemistry.