Ruprecht-Karls-Universitšt Heidelberg

Publications by the Bukau Lab (2003 - 1983)

see publications present - 2011
see publications 2010 - 2004
search pubmed for current publications by B. Bukau


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.
Mol Microbiol. 2003 50, 585-95.

Strub C, Schlieker C, Bukau B, Mogk A.

Poly-L-lysine enhances the protein disaggregation activity of ClpB.
FEBS Lett. 2003 553, 125-30.

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.
Mol Cell. 2003 12, 373-80.

Rist W, Jorgensen TJ, Roepstorff P, Bukau B, Mayer MP.

Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription
factor sigma 32 by amide hydrogen exchange.
J Biol Chem. 2003 278, 51415-21

Hengge R, Bukau B.

Proteolysis in prokaryotes: protein quality control and regulatory principles.
Mol Microbiol. 2003 49, 1451-62.

Weibezahn J, Schlieker C, Bukau B, Mogk A.

Characterization of a trap mutant of the AAA+ chaperone ClpB.
J Biol Chem. 2003 278, 32608-17.

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.
J Biol Chem. 2003 278, 31033-42.

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,
and chaperone activity.
J Biol Chem. 2003 278, 17615-24.

Deuerling E, Patzelt H, Vorderwulbecke S, Rauch T, Kramer G, Schaffitzel E, Mogk A, Schulze-Specking A,
Langen H, Bukau B.

Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.
Mol Microbiol. 2003 47, 1317-28.

Schlothauer T, Mogk A, Dougan DA, Bukau B, Turgay K.

MecA, an adaptor protein necessary for ClpC chaperone activity.
Proc Natl Acad Sci U S A. 2003 100, 2306-11.

Erbse A, Dougan DA, Bukau B.

A folding machine for many but a master of none.
Nat Struct Biol. 2003 10, 84-6.


Vandenbroeck, K, Alloza, I, Brehmer, D, Billiau, A, Proost, P, McFerran, N, Ruediger, S, and Walker, B.

The conserved Helix C region in the superfamily of the interferon-gamma/ Interleukin-10-related
cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK.
J. Cell. Biol. 2002 277, 25668-76.

Mayer MP, Nikolay R, Bukau B.

Aha, another regulator for hsp90 chaperones.
Mol Cell. 2002 10, 1255-6.

Dougan DA, Mogk A, Bukau B.

Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question.
Cell Mol Life Sci. 2002 59, 1607-16.

Mogk A, Mayer, MP, Deuerling E.

Mechanisms of protein folding: Molecular chaperones and their application in biotechnology.
ChemBioChem. 2002 3, 807-14.

Patzelt H, Kramer G, Rauch T, Schonfeld HJ, Bukau B, Deuerling E.

Three-state equilibrium of Escherichia coli trigger factor.
Biol Chem. 2002 383, 1611-9.

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.
Nat Struct Biol. 2002 9, 906-11.

Dougan DA, Mogk A, Zeth K, Turgay K, Bukau B.

AAA+ proteins and substrate recognition, it all depends on their partner in crime.
FEBS Lett. 2002 529: 6-10.

Kramer G, Rauch T, Rist W, Vorderwulbecke S, Patzelt H, Schulze-Specking A, Ban N, Deuerling E, Bukau B.

L23 protein functions as a chaperone docking site on the ribosome.
Nature 2002 419, 171-4.

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
Hsp70 chaperones.
J Biol Chem. 2002 277, 41060-9.

Mayer MP, Tomoyasu T, Bukau B.

[Molecular mechanism of Hsp70 chaperones]
Tanpakushitsu Kakusan Koso. 2002 47, 1189-95. RJapanese.

Schlieker C, Bukau B, Mogk A.

Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol:
implications for their applicability in biotechnology.
J Biotechnol. 2002 96, 13-21.

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
complex with the N-terminal domain of ClpA.
Acta Crystallogr D Biol Crystallogr. 2002 58(Pt 7), 1207-10.

Dougan DA, Reid BG, Horwich AL, Bukau B.

ClpS, a substrate modulator of the ClpAP machine.
Mol Cell. 2002 9, 673-83.

Wiederkehr T, Bukau B, Buchberger A.

Protein turnover: a CHIP programmed for proteolysis.
Curr Biol. 2002 12, R26-8.


Mayer MP, Brehmer D, Gassler CS, Bukau B.

Hsp70 chaperone machines.
Adv Protein Chem. 2001 59, 1-44.

Mogk A, Mayer MP, Deuerling E.

Molekulare Chaperone und ihr biotechnologisches Potential.
Biologie in unserer Zeit 2001 31, 182-92.

Patzelt H, Rudiger S, Brehmer D, Kramer G, Vorderwulbecke S, Schaffitzel E, Waitz A, Hesterkamp T,
Dong L, Schneider-Mergener J, Bukau B, Deuerling E.

Binding specificity of Escherichia coli trigger factor.
Proc Natl Acad Sci U S A. 2001 98, 14244-9.

Schaffitzel E, Rudiger S, Bukau B, Deuerling E.

Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and
thermally denatured proteins.
Biol Chem. 2001 382, 1235-43.

Tomoyasu T, Arsene F, Ogura T, Bukau B.

The C terminus of sigma(32) is not essential for degradation by FtsH.
J Bacteriol. 2001 183, 5911-7.

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
as positive and negative cofactor.
J Biol Chem. 2001 276: 32538-44.

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.
Nat Struct Biol. 2001 8, 427-32.

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
the Escherichia coli cytosol.
Mol Microbiol. 2001 40, 397-413.

Rudiger S, Schneider-Mergener J, Bukau B.

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.
EMBO J. 2001 20, 1042-50.


Rudiger S, Mayer MP, Schneider-Mergener J, Bukau B.

Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch.
J Mol Biol. 2000 304, 245-51.

Mayer MP, Rudiger S, Bukau B.

Molecular basis for interactions of the DnaK chaperone with substrates.
Biol Chem. 2000 381: 877-85.

Mayer MP, Schroder H, Rudiger S, Paal K, Laufen T, Bukau B.

Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
Nat Struct Biol. 2000 7, 586-93.

Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P.

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.
J Biol Chem. 2000 275, 21107-13.

Arsene F, Tomoyasu T, Bukau B.

The heat shock response of Escherichia coli.
Int J Food Microbiol. 2000 55. 3-9.

Bukau B, Deuerling E, Pfund C, Craig EA.

Getting newly synthesized proteins into shape.
Cell 2000 101, 119-22.


Buchberger A, Gassler CS, Buttner M, McMacken R, Bukau B.

Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles
for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.
J Biol Chem. 1999 274, 38017-26.

Deuerling E, Hesterkamp T, Bukau B.

Trigger Factor.
In: Encyclopedia of Molecular Biology 1999 2662-4 (Thomas E. Creighton, ed., John Wiley&Sons, Inc.).

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.
EMBO J. 1999 18, 6934-49.

Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B.

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.
Proc Natl Acad Sci U S A. 1999 96, 13732-7.

Knoblauch NT, Rudiger S, Schonfeld HJ, Driessen AJ, Schneider-Mergener J, Bukau B.

Substrate specificity of the SecB chaperone.
J Biol Chem. 1999 274, 34219-25.

Deuerling E, Schulze-Specking A, Tomoyasu T, Mogk A, Bukau B.

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.
Nature 1999 400, 693-6.

Mayer MP, Laufen T, Paal K, McCarty JS, Bukau B.

Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.
J Mol Biol. 1999 289, 1131-44.

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.
J Bacteriol. 1999 181, 3552-61.

Brix J, Rudiger S, Bukau B, Schneider-Mergener J, Pfanner N.

Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70
in a presequence-carrying preprotein and a non-cleavable preprotein.
J Biol Chem. 1999 274, 16522-30.

Mayer MP, Bukau B.

Molecular chaperones: the busy life of Hsp90.
Curr Biol. 1999 9, R322-5.

Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B.

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.
Proc Natl Acad Sci U S A. 1999 96, 5452-7.

Mogk A, Bukau B, Lutz R, Schumann W.

Construction and analysis of hybrid Escherichia coli-Bacillus subtilis dnaK genes.
J Bacteriol. 1999 181, 1971-4.


Ruediger S, Bukau B.

Bestimmung der Substratspezifitaet molekularer Chaperone mit Cellulose-gebundenen Peptiden.
Biospektrum. 1998 3, 35-37.

Zuber U, Buchberger A, Laufen A, Bukau B.

DnaJ Proteins.
In: Molecular Chaperones in the Life Cycle of Proteins 1998 (A.L. Fink&Y. Goto, eds) Marcel Dekker, Inc. 241-274.

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.
Proc Natl Acad Sci U S A. 1998 95, 15229-34.

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
control mechanisms of sigma32 in vivo.
Mol Microbiol. 1998 30, 583-93.

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.
Mol Microbiol. 1998 30, 567-81.

Hesterkamp T, Bukau B.

Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli.
EMBO J. 1998 17, 4818-28.

Mayer MP, Bukau B.

Hsp70 chaperone systems: diversity of cellular functions and mechanism of action.
Biol Chem. 1998 379. 261-8.

Bukau B, Horwich AL.

The Hsp70 and Hsp60 chaperone machines.
Cell 1998 92, 351-66.


Terada K, Kanazawa M, Bukau B, Mori M.

The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding.
J Cell Biol. 1997 139, 1089-95.

Hesterkamp T, Deuerling E, Bukau B.

The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary
and sufficient for binding to ribosomes.
J Biol Chem. 1997 272, 21865-71.

Shotland Y, Koby S, Teff D, Mansur N, Oren DA, Tatematsu K, Tomoyasu T, Kessel M, Bukau B, Ogura T, Oppenheim AB.

Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli.
Mol Microbiol. 1997 24, 1303-10.

Rudiger S, Buchberger A, Bukau B.

Interaction of Hsp70 chaperones with substrates.
Nat Struct Biol. 1997 4, 342-9. ]

Rudiger S, Germeroth L, Schneider-Mergener J, Bukau B.

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries.
EMBO J. 1997 16, 1501-7.

Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS, Reinstein J.

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative
displacement mechanism.
Biochemistry. 1997 36, 3417-22.


Bukau B, Schmid FX

Biochemie und Molekulargenektik 1996.
Nachr Chgem Tech Lab. 1996 2; 166-9

Theyssen H, Schuster HP, Packschies L, Bukau B, Reinstein J.

The second step of ATP binding to DnaK induces peptide release.
J Mol Biol. 1996 263, 657-70.

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.
J Mol Biol. 1996 261, 328-33.

Hesterkamp T, Bukau B.

The Escherichia coli trigger factor.
FEBS Lett. 1996 389, 32-4.

Hesterkamp T, Hauser S, Lutcke H, Bukau B.

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
Proc Natl Acad Sci U S A. 1996 93, 4437-41.

Bukau B, Hesterkamp T, Luirink J.

Growing up in a dangerous environment: a network of multiple targeting and folding pathways
for nascent polypeptides in the cytosol.
Trends Cell Biol. 1996 6; 480-486

Hesterkamp T, Bukau B.

Identification of the prolyl isomerase domain of Escherichia coli trigger factor.
FEBS Lett. 1996 385, 67-71.

Langer T, Buchner J, Bukau B.

Chaperone function on Crete: a meeting report.
Cell Stress Chaperones 1996 1, 5-12.

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
site and is conserved among eubacteria.
J Mol Biol. 1996 256, 829-37.

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
Escherichia coli heat shock transcription factor sigma32.
EMBO J. 1996 15, 607-17.


Levy EJ, McCarty J, Bukau B, Chirico WJ.

Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70
chaperones and modulators.
FEBS Lett. 1995 368, 435-40.

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
of the DnaK chaperone provide evidence for interdomain communication.
J Biol Chem. 1995 270, 16903-10.

Tomoyasu T, Gamer J, Bukau B, Kanemori M, Mori H, Rutman AJ, Oppenheim AB, Yura T, Yamanaka K, Niki H, et al.

Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.
EMBO J. 1995 14, 2551-60.

McCarty JS, Buchberger A, Reinstein J, Bukau B.

The role of ATP in the functional cycle of the DnaK chaperone system.
J Mol Biol. 1995 249, 126-37.

Schonfeld HJ, Schmidt D, Schroder H, Bukau B.

The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the
DnaK and GrpE components.
J Biol Chem. 1995 270, 2183-9.


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,
DnaJ, and GrpE.
Proc Natl Acad Sci U S A. 1994 91, 10345-9.

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.
EMBO J. 1994 13, 1687-95.

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.
Nat Struct Biol. 1994 1, 95-101.



Schroder H, Langer T, Hartl FU, Bukau B.

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
EMBO J. 1993 12, 4137-44.

Bukau B.

Regulation of the Escherichia coli heat-shock response.
Mol Microbiol. 1993 9, 671-80.

Bukau B, Reilly P, McCarty J, Walker GC.

Immunogold localization of the DnaK heat shock protein in Escherichia coli cells.
J Gen Microbiol. 1993 139 (Pt 1): 95-9.


Gamer J, Bujard H, Bukau B.

Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock
transcription factor sigma 32.
Cell. 1992 69, 833-42.

Bork P, Sander C, Valencia A, Bukau B.

A module of the DnaJ heat shock proteins found in malaria parasites.
Trends Biochem Sci. 1992 17, 129.


Bukau B, Walker GC.

E. coli mutants lacking the dnaK heat shock gene: Identification of cellular defects and analysis
of suppresor mutations.
In: Heat Shock 1991 Maresca B and Linquist S, Eds. pp 55-66.


Bukau B, Walker GC.

Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of
E. coli mutants lacking the DnaK chaperone.
EMBO J. 1990 9, 4027-36.


Bukau B, Walker GC.

Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid
maintenance at normal growth temperatures.
J Bacteriol. 1989 171, 6030-8.

Bukau B, Walker GC.

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock
protein in normal metabolism.
J Bacteriol. 1989 171, 2337-46.


Case CC, Bukau B, Granett S, Villarejo MR, Boos W.

Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli.
J Bacteriol. 1986 166, 706-12.

Bukau B, Ehrmann M, Boos W.

Osmoregulation of the maltose regulon in Escherichia coli.
J Bacteriol. 1986 166, 884-91.


Bukau B, Brass JM, Boos W.

Ca2+-induced permeabilization of the Escherichia coli outer membrane: comparison of transformation
and reconstitution of binding-protein-dependent transport.
J Bacteriol. 1985 163, 61-8.


Brass JM, Ehmann U, Bukau B.

Reconstitution of maltose transport in Escherichia coli: conditions affecting import of maltose-binding
protein into the periplasm of calcium-treated cells.
J Bacteriol. 1983 155, 97-106.