Bernd Bukau
Heidelberg University
Binding siteBiophysicsProtein aggregationChemistryProtein foldingHeat shock proteinATPaseCLPBSaccharomyces cerevisiaeProtein biosynthesisChaperone (protein)Protein structurePlasma protein bindingEscherichia coliBiochemistryHsp70BiologyRibosomeCell biologyCytosol
291Publications
119H-index
33.6kCitations
Publications 283
Newest
#1Joseph G. Beton (Heinrich Pette Institute)H-Index: 3
#2Jim Monistrol (Birkbeck, University of London)
Last. Helen R. Saibil (Birkbeck, University of London)H-Index: 79
view all 8 authors...
Although amyloid fibres are highly stable protein aggregates, a specific combination of human Hsp70 system chaperones can disassemble them, including fibres formed of α-synuclein, huntingtin or Tau. Disaggregation requires the ATPase activity of the constitutively expressed Hsp70, Hsc70, together with the J domain protein DNAJB1 and the nucleotide exchange factor Apg2. Recruitment and clustering of Hsc70 on the fibrils appear to be necessary for disassembly. Here we use atomic force microscopy (...
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#1Kevin Reinle (Heidelberg University)H-Index: 1
#2Axel Mogk (Heidelberg University)H-Index: 48
Last. Bernd Bukau (Heidelberg University)H-Index: 119
view all 3 authors...
Abstract null null The protein quality control (PQC) system maintains protein homeostasis by counteracting the accumulation of misfolded protein conformers. Substrate degradation and refolding activities executed by ATP-dependent proteases and chaperones constitute major strategies of the proteostasis network. Small heat shock proteins represent ATP-independent chaperones that bind to misfolded proteins, preventing their uncontrolled aggregation. sHsps share the conserved α-crystallin domain (AC...
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#2Mostafa Zedan (DKFZ: German Cancer Research Center)H-Index: 2
#3Bernd Hessling (DKFZ: German Cancer Research Center)H-Index: 10
Last. Bernd Bukau (DKFZ: German Cancer Research Center)H-Index: 119
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Summary N-terminal (Nt) acetylation is a highly prevalent co-translational protein modification in eukaryotes, catalyzed by at least five Nt acetyltransferases (Nats) with differing specificities. Nt acetylation has been implicated in protein quality control, but its broad biological significance remains elusive. We investigate the roles of the two major Nats of S. cerevisiae, NatA and NatB, by performing transcriptome, translatome, and proteome profiling of natAΔ and natBΔ mutants. Our results ...
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#1Anne S. Wentink (DKFZ: German Cancer Research Center)H-Index: 8
#2Nadinath B. Nillegoda (DKFZ: German Cancer Research Center)H-Index: 19
Last. Bernd Bukau (DKFZ: German Cancer Research Center)H-Index: 119
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#1Matilde Bertolini (DKFZ: German Cancer Research Center)H-Index: 1
#2Kai Fenzl (DKFZ: German Cancer Research Center)H-Index: 3
Last. Günter Kramer (DKFZ: German Cancer Research Center)H-Index: 33
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INTRODUCTION Most newly synthesized proteins associate into macromolecular complexes to become functional. Complex formation requires that subunits find each other in the crowded cellular environment while avoiding unspecific interactions and aggregation. Recent findings indicate that native complex formation is facilitated by coupling protein synthesis by ribosomes (translation) with folding and assembly. Studies analyzing formation of heteromeric complexes have elucidated the cotranslational e...
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#1Nabeel Ahmed (PSU: Pennsylvania State University)H-Index: 6
#2Ulrike A. Friedrich (DKFZ: German Cancer Research Center)H-Index: 4
Last. Edward P. O'Brien (PSU: Pennsylvania State University)H-Index: 30
view all 8 authors...
Variation in translation-elongation kinetics along a transcript's coding sequence plays an important role in the maintenance of cellular protein homeostasis by regulating co-translational protein folding, localization, and maturation. Translation-elongation speed is influenced by molecular factors within mRNA and protein sequences. For example, the presence of proline in the ribosome's P- or A-site slows down translation, but the effect of other pairs of amino acids, in the context of all 400 po...
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#1Bernd Bukau (Heidelberg University)H-Index: 119
#2Michael Lanzer (Heidelberg University)H-Index: 56
Last. Gerlind Wallon (European Molecular Biology Organization)H-Index: 5
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#1Ofrah Faust (Weizmann Institute of Science)H-Index: 2
#2Meital Abayev-Avraham (Weizmann Institute of Science)H-Index: 1
Last. Rina Rosenzweig (Weizmann Institute of Science)H-Index: 20
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The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular chaperones, which perform numerous cellular functions that affect almost all aspects of the protein life cycle from synthesis to degradation1-3. Achieving this broad spectrum of functions requires precise regulation of HSP70 activity. Proteins of the HSP40 family, also known as J-domain proteins (JDPs), have a key role in this process by preselecting substrates for transfer to their HSP70 partners and by stim...
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#1Anne S. Wentink (DKFZ: German Cancer Research Center)H-Index: 8
#2Nadinath B. Nillegoda (DKFZ: German Cancer Research Center)H-Index: 19
Last. Bernd Bukau (DKFZ: German Cancer Research Center)H-Index: 119
view all 9 authors...
The deposition of highly ordered fibrillar-type aggregates into inclusion bodies is a hallmark of neurodegenerative diseases such as Parkinson's disease. The high stability of such amyloid fibril aggregates makes them challenging substrates for the cellular protein quality-control machinery1,2. However, the human HSP70 chaperone and its co-chaperones DNAJB1 and HSP110 can dissolve preformed fibrils of the Parkinson's disease-linked presynaptic protein α-synuclein in vitro3,4. The underlying mech...
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#1Jonathan Bohlen (DKFZ: German Cancer Research Center)H-Index: 4
#2Liza Harbrecht (DKFZ: German Cancer Research Center)H-Index: 1
Last. Aurelio A. Teleman (DKFZ: German Cancer Research Center)H-Index: 35
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Translation efficiency varies considerably between different mRNAs, thereby impacting protein expression. Translation of the stress response master-regulator ATF4 increases upon stress, but the molecular mechanisms are not well understood. We discover here that translation factors DENR, MCTS1 and eIF2D are required to induce ATF4 translation upon stress by promoting translation reinitiation in the ATF4 5'UTR. We find DENR and MCTS1 are only needed for reinitiation after upstream Open Reading Fra...
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