Bernd Bukau

This study shows how phase separation alters the conformational dynamics of DNAJB1, priming it for HSP70 binding and stress granule disassembly.

The paper identifies small-molecule activators of the Staphylococcus aureus ClpC/ClpP protease through high-throughput screening and characterizes their binding sites.

The paper shows that the ribosome coordinates folding and assembly of a complex protein to enable efficient biogenesis.

This study investigates co-translational assembly of homomeric proteins, showing that PheA in E. coli primarily assembles via trans-assembly across neighboring mRNAs.

This study shows that the thermodynamic stability of alpha-synuclein fibrils affects their disaggregation by the chaperone system HSP70, DNAJB1, and Apg2, with more stable fibrils being less efficiently disaggregated.

The paper shows that different structures of alpha-synuclein fibrils affect how Hsc70 chaperones disaggregate them, influencing protein quality control and aggregation.

This study identifies Apj1 and Ydj1 as J-domain proteins that regulate Hsf1 in distinct phases of the heat shock response in yeast.

This paper introduces a new ribosome profiling protocol that is faster, cheaper, and more sensitive, enabling use with minimal RNA input.

The paper reveals a temporal control mechanism driven by coupled ribosomes that enables the formation of intertwined protein dimers by bypassing closed monomeric states.

The paper shows co-translational ribosome pairing enables the formation of coiled-coil homodimers from misfolding-prone subunits through chaperone-like interactions between nascent chains.

The paper identifies NAC's role in promoting co-translational folding by interacting with nascent chains at the ribosomal tunnel exit, expanding its known functions in protein biogenesis.

This study shows DNAJB1 recruits Hsc70 in two steps to amyloid fibers, forming ordered arrays that enable efficient disaggregation, while a mutant disrupts this organization.

This study identifies a unique chaperoning mechanism in class-A JDPs that recognizes and stabilizes mutant p53, promoting cancer progression by preventing its degradation.

The paper investigates the distinct physiological roles of NatA and NatB in S. cerevisiae through transcriptome, translatome, and proteome profiling of mutants, revealing specific effects on gene expression and protein folding.

The paper identifies amino acid pairs at the ribosome's P- and A-sites that predictably and causally modulate translation-elongation rates in yeast.

This paper introduces selective 40S footprinting to study translation initiation in human cells, revealing that scanning ribosomes remain cap-tethered and only one ribosome scans a 5UTR at a time.

This study shows that the Hsp70 disaggregation machinery disassembles Tau fibrils, generating small seeding-competent Tau species that can drive aggregation.

The paper identifies Bfr1 as a regulator of Pmt1 and Pmt2 translation, affecting unfolded protein O-mannosylation in yeast.

The paper identifies a new quality control pathway for integral membrane proteins involving RAC-Ssb that couples translation rate to the unfolded protein response.

This study evaluates how green fluorescent protein (greenFP) maturation kinetics and proteasomal degradation affect tandem fluorescent protein timers (tFTs), identifying greenFPs that degrade efficiently and guidelines for tFT design.