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Publications by the Bukau Lab (2003 - 1983)
Mogk A, Deuerling E, Vorderwulbecke S, Vierling E, Bukau B. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Poly-L-lysine enhances the protein disaggregation activity of ClpB. Dougan DA, Weber-Ban E, Bukau B. Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Rist W, Jorgensen TJ, Roepstorff P, Bukau B, Mayer MP. Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription Proteolysis in prokaryotes: protein quality control and regulatory principles. Weibezahn J, Schlieker C, Bukau B, Mogk A. Characterization of a trap mutant of the AAA+ chaperone ClpB. Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E, Bukau B. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, Deuerling E, Patzelt H, Vorderwulbecke S, Rauch T, Kramer G, Schaffitzel E, Mogk A, Schulze-Specking A, Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Schlothauer T, Mogk A, Dougan DA, Bukau B, Turgay K. MecA, an adaptor protein necessary for ClpC chaperone activity. A folding machine for many but a master of none. 2002 The conserved Helix C region in the superfamily of the interferon-gamma/ Interleukin-10-related Aha, another regulator for hsp90 chaperones. Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. Mogk A, Mayer, MP, Deuerling E. Mechanisms of protein folding: Molecular chaperones and their application in biotechnology. Patzelt H, Kramer G, Rauch T, Schonfeld HJ, Bukau B, Deuerling E. Three-state equilibrium of Escherichia coli trigger factor. Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA. Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Dougan DA, Mogk A, Zeth K, Turgay K, Bukau B. AAA+ proteins and substrate recognition, it all depends on their partner in crime. L23 protein functions as a chaperone docking site on the ribosome. Kluck CJ, Patzelt H, Genevaux P, Brehmer D, Rist W, Schneider-Mergener J, Bukau B, Mayer MP. Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Mayer MP, Tomoyasu T, Bukau B. [Molecular mechanism of Hsp70 chaperones] Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Zeth K, Dougan DA, Cusack S, Bukau B, Ravelli RB. Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in Dougan DA, Reid BG, Horwich AL, Bukau B. ClpS, a substrate modulator of the ClpAP machine. Wiederkehr T, Bukau B, Buchberger A. Protein turnover: a CHIP programmed for proteolysis.
Mayer MP, Brehmer D, Gassler CS, Bukau B. Hsp70 chaperone machines. Mogk A, Mayer MP, Deuerling E. Molekulare Chaperone und ihr biotechnologisches Potential. Patzelt H, Rudiger S, Brehmer D, Kramer G, Vorderwulbecke S, Schaffitzel E, Waitz A, Hesterkamp T, Binding specificity of Escherichia coli trigger factor. Schaffitzel E, Rudiger S, Bukau B, Deuerling E. Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and Tomoyasu T, Arsene F, Ogura T, Bukau B. The C terminus of sigma(32) is not essential for degradation by FtsH. Gassler CS, Wiederkehr T, Brehmer D, Bukau B, Mayer MP. Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent Brehmer D, Rudiger S, Gassler CS, Klostermeier D, Packschies L, Reinstein J, Mayer MP, Bukau B. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in Rudiger S, Schneider-Mergener J, Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. 2000 Rudiger S, Mayer MP, Schneider-Mergener J, Bukau B. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. Molecular basis for interactions of the DnaK chaperone with substrates. Mayer MP, Schroder H, Rudiger S, Paal K, Laufen T, Bukau B. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. Arsene F, Tomoyasu T, Bukau B. The heat shock response of Escherichia coli. Bukau B, Deuerling E, Pfund C, Craig EA. Getting newly synthesized proteins into shape.
Buchberger A, Gassler CS, Buttner M, McMacken R, Bukau B. Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles Deuerling E, Hesterkamp T, Bukau B. Trigger Factor. Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, Bukau B. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Knoblauch NT, Rudiger S, Schonfeld HJ, Driessen AJ, Schneider-Mergener J, Bukau B. Substrate specificity of the SecB chaperone. Deuerling E, Schulze-Specking A, Tomoyasu T, Mogk A, Bukau B. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Mayer MP, Laufen T, Paal K, McCarty JS, Bukau B. Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. Arsene F, Tomoyasu T, Mogk A, Schirra C, Schulze-Specking A, Bukau B. Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32. Brix J, Rudiger S, Bukau B, Schneider-Mergener J, Pfanner N. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 Molecular chaperones: the busy life of Hsp90. Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B. Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Mogk A, Bukau B, Lutz R, Schumann W. Construction and analysis of hybrid Escherichia coli-Bacillus subtilis dnaK genes. Bestimmung der Substratspezifitaet molekularer Chaperone mit Cellulose-gebundenen Peptiden. Zuber U, Buchberger A, Laufen A, Bukau B. DnaJ Proteins. Gassler CS, Buchberger A, Laufen T, Mayer MP, Schroder H, Valencia A, Bukau B. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Tatsuta T, Tomoyasu T, Bukau B, Kitagawa M, Mori H, Karata K, Ogura T. Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity Tomoyasu T, Ogura T, Tatsuta T, Bukau B. Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli. Hsp70 chaperone systems: diversity of cellular functions and mechanism of action. The Hsp70 and Hsp60 chaperone machines. 1997 Terada K, Kanazawa M, Bukau B, Mori M. The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. Hesterkamp T, Deuerling E, Bukau B. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli. Rudiger S, Buchberger A, Bukau B. Interaction of Hsp70 chaperones with substrates. Rudiger S, Germeroth L, Schneider-Mergener J, Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS, Reinstein J. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative Bukau B, Schmid FX Biochemie und Molekulargenektik 1996. Theyssen H, Schuster HP, Packschies L, Bukau B, Reinstein J. The second step of ATP binding to DnaK induces peptide release. Buchberger A, Schroder H, Hesterkamp T, Schonfeld HJ, Bukau B. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. The Escherichia coli trigger factor. Hesterkamp T, Hauser S, Lutcke H, Bukau B. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Bukau B, Hesterkamp T, Luirink J. Growing up in a dangerous environment: a network of multiple targeting and folding pathways Identification of the prolyl isomerase domain of Escherichia coli trigger factor. Chaperone function on Crete: a meeting report. McCarty JS, Rudiger S, Schonfeld HJ, Schneider-Mergener J, Nakahigashi K, Yura T, Bukau B. Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rudiger S, Schonfeld HJ, Schirra C, Bujard H, Bukau B. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the 1995 Levy EJ, McCarty J, Bukau B, Chirico WJ. Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 Buchberger A, Theyssen H, Schroder H, McCarty JS, Virgallita G, Milkereit P, Reinstein J, Bukau B. Nucleotide-induced conformational changes in the ATPase and substrate binding domains Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. McCarty JS, Buchberger A, Reinstein J, Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. Schonfeld HJ, Schmidt D, Schroder H, Bukau B. The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the Szabo A, Langer T, Schroder H, Flanagan J, Bukau B, Hartl FU. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, Buchberger A, Valencia A, McMacken R, Sander C, Bukau B. The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. Buchberger A, Schroder H, Buttner M, Valencia A, Bukau B. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.
1993 Schroder H, Langer T, Hartl FU, Bukau B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. Regulation of the Escherichia coli heat-shock response. Bukau B, Reilly P, McCarty J, Walker GC. Immunogold localization of the DnaK heat shock protein in Escherichia coli cells.
Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock Bork P, Sander C, Valencia A, Bukau B. A module of the DnaJ heat shock proteins found in malaria parasites. 1991 Bukau B, Walker GC. E. coli mutants lacking the dnaK heat shock gene: Identification of cellular defects and analysis 1990 Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of 1989 Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock 1986 Case CC, Bukau B, Granett S, Villarejo MR, Boos W. Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli. Osmoregulation of the maltose regulon in Escherichia coli.
Ca2+-induced permeabilization of the Escherichia coli outer membrane: comparison of transformation 1983 Reconstitution of maltose transport in Escherichia coli: conditions affecting import of maltose-binding |
