Ruprecht-Karls-Universität Heidelberg

Publications by the Bukau Lab (present - 2011)

see publications 2010 - 2004
see publications 2003 - 1983
search pubmed for current publications by B. Bukau


Deville, C., Carroni, M., Franke, K.B., Topf, M., Bukau, B., Mogk, A., Saibil, H.R. Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. (2017) Sci Adv. 3:e1701726. doi: 10.1126/sciadv.1701726. (Abstract).

Zemva, J., Fink, C.A., Fleming, T.H., Schmidt, L., Loft, A., Herzig, S., Knieß, R.A., Mayer, M., Bukau, B., Nawroth, P.P., Tyedmers, J. Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux. (2017) Redox Biol. 13:674-686. doi: 10.1016/j.redox.2017.08.007. (Abstract).

Döring, K., Ahmed, N., Riemer, T., Suresh, H.G., Vainshtein, Y., Habich, M., Riemer, J., Mayer, M.P., O'Brien, E.P., Kramer, G., Bukau, B. Profiling Ssb-nascent chain interactions reveals principles of Hsp70-assisted folding. (2017) Cell 170:298-311.e20. doi: 10.1016/j.cell.2017.06.038. (Abstract).

Bascos, N.A.D., Mayer, M.P., Bukau, B., Landry, S.J. The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring. (2017) Protein Sci. doi: 10.1002/pro.3223 (Epub ahead of print). (Abstract).

Garcia, V.M., Nillegoda, N.B., Bukau, B., Morano, K.A. Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone, Sse1, is not obligate for its biological activities. (2017) Mol. Biol. Cell pii: mbc.E17-01-0070. doi: 10.1091/mbc.E17-01-0070. Epub ahead of print. (Abstract).

Nillegoda, N.B., Stank, A., Malinverni, D., Alberts, N., Szlachcic, A., Barducci, A., De Los Rios, P., Wade, R.C., Bukau, B. Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes. (2017) Elife doi: 10.7554/eLife.24560. (Abstract).

Carra, S., Alberti, S., Arrigo, P.A., , Benesch, J.L., Benjamin, I.J., Boelens, W., Bartelt-Kirbach, B., Brundel, B.J., Buchner, J., Bukau, B., Carver, J.A., Ecroyd, H., Emanuelsson, C., Finet, S., Golenhofen, N., Goloubinoff, P., Gusev, N., Haslbeck, M., Hightower, L.E., Kampinga, H.H., Klevit, R.E., Liberek, K., Mchaourab, H.S., McMenimen, K.A., Poletti, A., Quinlan, R., Strelkov, S.V., Toth, M.E., Vierling, E., Tanguay, R.M. The growing world of small heat shock proteins: from structure to functions. (2017) Cell Stress & Chaperones doi: 10.1007/s12192-017-0787-8 (Abstract).

Franke, K.B., Bukau, B.,Mogk, A. Mutant analysis reveals allosteric regulation of ClpB disaggregase. (2017) Front. Mol. Biosci. doi: 10.3389/fmolb.2017.00006 (Abstract).

Zwirowski S, Klosowska A, Obuchowski I, Nillegoda NB, Piróg A, Zietkiewicz S, Bukau B, Mogk A, Liberek K. Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding. (2017) EMBO J. 36, 783-796. doi: 10.15252/embj.201593378. (Abstract).

Mogk, A. and Bukau, B. Role of sHsps in organizing cytosolic protein aggregation and disaggregation. (2017) Cell Stress & Chaperones doi: 10.1007/s12192-017-0762-4. [Epub ahead of print] (Abstract).


Ungelenk, S., Moayed, F., Ho, C.T., Grousl, T., Scharf, A., Mashaghi, A., Tans, S., Mayer, M.P., Mogk, A., Bukau, B. Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding. (2016) Nat. Commun. 7, 13673 (Abstract).

Goerke, S., Milde, K.S., Bukowiecki, R., Kunz, P., Klika, K.D., Wiglenda, T., Mogk, A., Wanker, E.E., Bukau, B., Ladd, M.E., Bachert, P., Zaiss, M. Aggregation-induced changes in the chemical exchange saturation transfer (CEST) signals of proteins. (2016) NMR Biomed. doi: 10.1002/nbm.3665. (Abstract).

Mashaghi, A., Bezrukavnikov, S., Minde, D.P., Wentink, A.S., Kityk, R., Zachmann-Brand, B., Mayer, M.P., Kramer, G., Bukau, B., Tans, S.J. Alternative modes of client binding enable functional plasticity of Hsp70. (2016) Nature 539, 448-451 (Abstract).

Huber, D., Jamshad, M., Hanmer, R., Schibich, D., Döring, K., Marcomini, I., Kramer, G., Bukau, B. SecA cotranslationally interacts with nascent substrate proteins in vivo. (2016) J. Bacteriol. pii: JB.00622-16. Epub ahead of print. (Abstract).

Kummer, E., Szlachcic, A., Franke, K.B., Ungelenk, S., Bukau, B., Mogk, A. Bacterial and yeast AAA+ disaggregases ClpB and Hsp104 operate through conserved mechanism involving cooperation with Hsp70. (2016) J. Mol. Biol. 428, 4378-4391 (Abstract).

Lange, S., Franks, W.T., Rajagopalan, N., Döring, K., Geiger, M.A., Linden, A., van Rossum, B.J., Kramer, G., Bukau, B., Oschkinat, H. Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR. (2016) Sci. Adv. 2, e1600379. doi: 10.1126/sciadv.1600379. eCollection 2016 Aug. (Abstract).

Schibich, D., Gloge, F., Pöhner, I., Björkholm, P., Wade, R.C., von Heijne, G., Bukau, B., Kramer, G. Global profiling of SRP interaction with nascent polypeptides. (2016) Nature 536, 219-223, doi: 10.1038/nature19070 (Abstract).

Yonashiro, R., Tahara, E.B., Bengtson, M.H., Khokhrina, M., Lorenz, H., Chen, K.C., Kigoshi-Tansho, Y., Savas, J.N., Yates, J.R., Kay, S.A., Craig, E.A., Mogk, A., Bukau, B., Joazeiro, C.A. The Rqc2/Tae2 subunit of the Ribosome-Associated Quality Control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation. (2016) Elife pii: e11794. doi: 10.7554/eLife.11794. (Abstract)

Nilsson, O.B., Müller-Lucks, A., Kramer, G., Bukau, B., von Heijne, G. Trigger factor reduces the force exerted on the nascent chain by a cotranslationally folding protein. (2016) J. Mol. Biol. 428, 1356-1364, pii: S0022-2836(16)00130-3. doi: 10.1016/j.jmb.2016.02.014. (Abstract)

Nissley, D.A., Sharma, A.K., Ahmed, N., Friedrich, U.A., Kramer, G., Bukau, B., O'Brien, E.P. Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding. (2016) Nat. Commun. 7, 10341. doi: 10.1038/ncomms10341. (Abstract)

Sharma, A.K., Bukau, B., O'Brien, E.P. Physical Origins of Codon Positions That Strongly Influence Cotranslational Folding: A Framework for Controlling Nascent-Protein Folding. (2016) J. Am. Chem. Soc. 138, 11801195. doi: 10.1021/jacs.5b08145. (Abstract)

Khmelinskii, A., Meurer, M., Ho, C.T., Besenbeck, B., Füller, J., Lemberg, M.K., Bukau, B., Mogk, A., Knop, M. Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers. (2016) Mol. Biol. Cell 27, 360 - 370. (Abstract)


Nillegoda, N.B., Bukau B. Metazoan Hsp70-based protein disaggregases: emergence and mechanisms. (2015) Front. Mol. Biosci. doi: 10.3389/fmolb.2015.00057. eCollection 2015. Review. (Abstract)

Tryggvesson, A., Ståhlberg, F.M., Töpel, M., Tanabe, N., Mogk, A., Clarke, A.K. Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus. (2015) FEBS Lett. doi: 589(24 Pt B):4039-4046. doi: 10.1016/j.febslet.2015.11.026. (Abstract)

Cherkasov, V., Grousl, T., Theer, P., Vainshtein, Y., Gläßer, C., Mongis, C., Kramer, G., Stoecklin, G., Knop, M., Mogk, A., Bukau, B. Systemic control of protein synthesis through sequestration of translation and ribosome biogenesis factors during severe heat stress. (2015) FEBS Lett. 589, 3654-3664. doi: 10.1016/j.febslet.2015.10.010. (Abstract).

Shieh, Y.-W., Minguez, P., Bork, P., Auburger, J.J., Guilbride, D.L., Kramer, G., Bukau, B. Operon structure and cotranslational subunit association direct protein assembly in bacteria. (2015) Science 350, 678 - 680 (Abstract).

Kityk, R., Vogel, M., Schlecht, R., Bukau, B., Mayer, M.P. Pathways of allosteric regulation in Hsp70 chaperones. (2015) Nat. Commun. 6, 8308, doi: 10.1038/ncomms9308. (Abstract).

Gao, X., Carroni, M., Nussbaum-Krammer, C., Mogk, A., Nillegoda, N.B., Szlachcic, A., Guilbride, D.L., Saibil, H.R. Mayer, M.P., Bukau, B. Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils. (2015) Mol. Cell 59, 781-793. doi: 10.1016/j.molcel.2015.07.012 (Abstract).

Nillegoda, N.B., Kirstein, J., Szlachcic, A., Berynskyy, M., Stank, A., Stengel, F., Arnsburg, K., Gao, X., Scior, A., Aebersold, R., Guilbride, D.L., Wade, R.C., Morimoto, R.I., Mayer, M.P., Bukau, B. Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. (2015) Nature 524, 247 - 251, doi:10.1038/nature14884 (read more).

Kramer, G., Bukau, B. 18 The busy life of nascent chains: mechanisms of folding of newly synthesized proteins. (2015) J. Biomol. Struct. Dyn. 33 Suppl 1:10. doi: 10.1080/07391102.2015.1032558 (Abstract).

Mogk, A., Kummer, E., Bukau, B. Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation. (2015) Front. Mol. Biosci. 2, 22, doi: 10.3389/fmolb.2015.00022. eCollection 2015. (Abstract).

Goerke, S., Zaiss, M., Kunz, P., Klika, K.D., Windschuh, J.D., Mogk, A., Bukau, B., Ladd, M.E., Bachert, P. Signature of protein unfolding in chemical exchange saturation transfer imaging. (2015) NMR Biomed. 28, 906-913. (Abstract).

Garadi Suresh, H., Xavier da Silveira dos Santos, A., Kukulski, W., Tyedmers, J., Riezman, H., Bukau, B., Mogk, A. Prolonged starvation drives reversible sequestration of lipid biosynthetic enzymes and organelle reorganization in Saccharomyces cerevisiae. (2015) Mol. Biol. Cell 26, 1601-1615 (Abstract).

Kramer, G., Guilbride, D.L., Bukau, B. Cell Biology. Finding nascent proteins the right home. (2015) Science 348, 182-183 (Summary | Full text | Reprint).

Miller, S.B., Ho, C.T., Winkler, J., Khokhrina, M., Neuner, A., Mohamed, M.Y., Guilbride, D.L., Richter, K., Lisby, M., Schiebel, E., Mogk, A., Bukau, B. Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition. (2015) EMBO J. 34, 778-797. (Abstract)

Miller, S.B.M., Mogk, A., Bukau, B. Spatially organized aggregation of misfolded proteins as cellular stress defense strategy. (2015) J. Mol. Biol. 427, 1564-1574. (Abstract).


Mogk, A., Bukau, B. Mitochondria tether protein trash to rejuvenate cellular environments. (2014) Cell 159: 471-472 (Article).

Hsieh T.Y., Nillegoda, N.B., Tyedmers, J., Bukau, B., Mogk, A., Kramer, G. Monitoring protein misfolding by site-specific labeling of proteins in vivo. (2014) Plos One 9(6):e99395 (Abstract).

Carroni, M., Kummer, E., Oguchi, Y., Wendler, P., Clare, D.K., Sinning, I., Kopp, J., Mogk, A., Bukau, B., Saibil, H.R. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. (2014) Elife doi: 10.7554/eLife.02481 (Abstract).

Gloge, F., Becker, A.H., Kramer, G., Bukau, B. Co-translational mechanisms of protein maturation. (2014) Curr. Opin. Struct. Biol. 24, 24-33 (Abstract).


Cherkasov, V., Hofmann, S., Druffel-Augustin, S., Mogk, A., Tyedmers, J., Stoecklin, G., Bukau, B. Coordination of Translational Control and Protein Homeostasis during Severe Heat Stress. (2013) Curr. Biol. 23, 2452-2462 (Abstract).

Schlecht, R. Scholz, S.R., Dahmen, H., Wegener, A., Sirrenberg, C., Musil, D., Bomke, J., Eggenweiler, H.M., Mayer, M.P., Bukau, B. Functional analysis of hsp70 inhibitors. (2013) PLoS One 8(11), e78443 (Abstract). Correction.

Stoecklin, G., Bukau, B. Telling right from wrong in life - cellular quality control. (2013) Nat. Rev. Mol. Cell Biol. 14, 613-615 (Abstract).

Becker, A.H., Oh, E., Weissman, J. S., Kramer, G., Bukau, B. Selective ribosome profiling as a tool to study the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes. (2013) Nature Protocols 8, 2212-2239 (Abstract).

Mashaghi, A., Kramer, G., Bechtluft, P., Zachmann-Brand, B., Driessen, A. J., Bukau, B., Tans, S. J. Reshaping of the conformational search of a protein by the chaperone trigger factor. (2013) Nature 500, 98-101 (Abstract).

Sandikci, A., Gloge, F., Martinez, M., Mayer, M.P., Wade, R., Bukau, B., Kramer, G. Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding. (2013) Nat. Struct. Mol. Biol. 20, 843-850 (Abstract).

Tariq, M., Wegrzyn, R., Anwar, S., Bukau, B., Paro, R. Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior. (2013) BMC Genomics 14, 374 (Abstract).

Kummer, E., Oguchi, Y., Seyffer, F., Bukau, B., Mogk, A. Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride. (2013) FEBS Lett. 587, 810-817 (Abstract).


Oguchi, Y., Kummer, E., Seyffer, F., Berynskyy, M., Anstett, B., Zahn, R., Wade, R.C. Mogk, A., Bukau, B. A tightly regulated molecular toggle controls AAA+ disaggregase. (2012) Nat. Struct. Mol. Biol. 19, 1338-1346 (Abstract).

Seyffer, F., Kummer, E., Oguchi, Y., Winkler, J., Kumar, M., Zahn, R., Sourjik, V., Bukau, B., Mogk, A. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. (2012) Nat. Struct. Mol. Biol. 19, 1347-1355 (Abstract).

Rampelt, H., Kirstein-Miles, J., Nillegoda, N.B., Chi, K., Scholz., S.R., Morimoto, R.I., Bukau, B. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. (2012) EMBO J. 31, 4221-4235 (Abstract).

Hoffmann, A., Becker, A.H., Zachmann-Brand, B., Deuerling, E., Bukau, B., Kramer, G. Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding. (2012) Mol. Cell 48, 63-74 (Abstract).

Hofmann, S., Cherkasova, V., Bankhead, P., Bukau, B., Stoecklin, G. Translation suppression promotes stress granule formation and cell survival in response to cold shock. (2012) Mol. Biol. Cell 23, 3786-3800 (Abstract).

Winkler, J., Tyedmers, J., Bukau, B., Mogk, A. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. (2012) J. Cell Biol. 198, 387-404 (Abstract).

Winkler, J., Tyedmers, J., Bukau, B., Mogk, A. Chaperone networks in protein disaggregation and prion propagation. (2012) J. Struct. Biol. 179, 152-160 (Abstract).


Oh, E., Becker, A.H., Sandikci, A., Huber, D., Chaba, R., Gloge, F., Nichols, R.J., Typas, A., Gross, C.A., Kramer, G., Weissman, J.S., Bukau, B. Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo. (2011) Cell 147, 1295-1308 (Abstract).

Specht, S., Miller, S.B.M., Mogk, A., Bukau, B. Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. (2011) J. Cell Biol. 195, 617-629 (Abstract).

Rampelt, H., Mayer, M.P., Bukau, B. Nucleotide exchange factors for Hsp70 chaperones. In "Molecular chaperones: From protein quality control to physiological function", Series "Methods in Molecular Biology. S. Calderwood (Ed) ) (2011) 787, 83-91. (Abstract).

Kohl, C., Tessarz, P., von der Malsburg, K., Zahn, R., Bukau, B., Mogk, A. Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins. (2011) Biol. Chem. 392, 601-608. (Abstract).

Schlecht, R., Erbse, A., Bukau, B., Mayer, M.P. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. (2011) Nat. Struct. Mol. Biol. 18, 345-351 (Abstract).

Huber, D., Rajagopalan, N., Preissler, S., Rocco, M.A., Merz, F., Kramer, G., Bukau, B. SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria. (2011) Mol. Cell 41, 343-353 (Abstract).

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