KEY PUBLICATIONS

Alternative modes of client binding enable functional plasticity of Hsp70
Alireza Mashaghi et al. | Nature 539, 448-451 (2016) | pdf & DOI: 10.1038/nature20137
Stochasticity of metabolism and growth at the single-cell level
Daniel J. Kiviet et al. | Nature 514, 376-379 (2014) | pdf & DOI: 10.1038/nature13582
Reshaping of the conformational search of a protein by the chaperone trigger factor
Alireza Mashaghi et al. | Nature 500, 98-101 (2013) | pdf & DOI: 10.1038/nature12293
Tradeoffs and optimality in the evolution of gene regulation
Frank J. Poelwijk et al. | Cell 146, 462-470 (2011) | pdf & DOI:10.1016/j.cell.2011.06.035
Direct Observation of Chaperone-Induced Changes in a Protein Folding Pathway
Philipp Bechtluft, Ruud van Leeuwen et al. | Science 318:1458-1461 (2007) | pdf & DOI:10.1126/science.1144972
Empirical fitness landscapes reveal accessible evolutionary paths
Frank Poelwijk, Daan Kiviet et al. | Nature 445:383-386 (2007) | pdf & DOI:10.1038/nature05451
The bacteriophage phi29 portal motor can package DNA against a large internal force
Douglas E. Smith, Sander J. Tans et al. | Nature 413:748-52 (2001) | pdf & DOI:10.1038/35099581
Molecular transistors: Potential modulations along carbon nanotubes
Sander J. Tans, Cees Dekker. | Nature 404:834-35 (2000) | pdf & DOI:10.1038/35009026
Imaging electron wave functions of quantized energy levels in carbon nanotubes
Liesbeth C. Venema et al. | Science 283:52-55 (1999) | pdf & DOI:10.1126/science.283.5398.52
Electron-electron correlations in carbon nanotubes
Sander J. Tans et al. | Nature 394:761-64 (1998) | pdf & DOI:10.1038/29494
Room-temperature transistor based on a single carbon nanotube
Sander J. Tans, Alwin R. M. Verschueren & Cees Dekker | Nature 393:49-52 (1998) | pdf & DOI:10.1038/29954
Individual single-wall carbon nanotubes as quantum wires
Sander J. Tans et al. | Nature 386:474-77 (1997) | pdf & DOI:10.1038/386474a0
Fullerene 'crop circles'
Jie Liu et al. | Nature 385, 780-781 (1997) | pdf & DOI:10.1038/385780b0

Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding

Ungelenk, S.; Moayed, F.; Ho, C. T.; Grousl, T.; Scharf, A.; Mashaghi, A.; Tans, S.; Mayer, M. P.; Mogk, A.; Bukau, B.
Abstract:
Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of chaperones acting as first line of defence against proteotoxic stress. sHsps coaggregate with misfolded proteins but the molecular basis and functional implications of these interactions, as well as potential sHsp specific differences, are poorly explored. In a comparative analysis of the two yeast sHsps, Hsp26 and Hsp42, we show in vitro that model substrates retain near-native state and are kept physically separated when complexed with either sHsp, while being completely unfolded when aggregated without sHsps. Hsp42 acts as aggregase to promote protein aggregation and specifically ensures cellular fitness during heat stress. Hsp26 in contrast lacks aggregase function but is superior in facilitating Hsp70/Hsp100-dependent post-stress refolding. Our findings indicate the sHsps of a cell functionally diversify in stress defence, but share the working principle to promote sequestration of misfolding proteins for storage in native-like conformation.
Year:
2016
Type of Publication:
Article
Journal:
Nat Commun
Volume:
7
Pages:
13673
Month:
11
Note:
[PubMed Central:\href{https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5141385}{PMC5141385}] [DOI:\href{https://dx.doi.org/10.1038/ncomms13673}{10.1038/ncomms13673}] [PubMed:\href{https://www.ncbi.nlm.nih.gov/pubmed/27901028}{27901028}]
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