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  1. Article

    Open Access

    Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast

    The guided entry of tail-anchored proteins (GET) pathway assists in the posttranslational delivery of tail-anchored proteins, containing a single C-terminal transmembrane domain, to the ER. Here we uncover how...

    Ying Zhang, Evelina De Laurentiis, Katherine E. Bohnsack in Nature Communications (2021)

  2. Article

    Open Access

    The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb

    The conserved ribosome-associated complex (RAC) consisting of Zuo1 (Hsp40) and Ssz1 (non-canonical Hsp70) acts together with the ribosome-bound Hsp70 chaperone Ssb in de novo protein folding at the ribosomal t...

    Ying Zhang, Genís Valentín Gesé, Charlotte Conz, Karine Lapouge in Nature Communications (2020)

  3. No Access

    Article

    Function, evolution, and structure of J-domain proteins

    Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation o...

    Harm H. Kam**a, Claes Andreasson, Alessandro Barducci in Cell Stress and Chaperones (2019)

  4. Article

    Open Access

    The Hsp70 homolog Ssb affects ribosome biogenesis via the TORC1-Sch9 signaling pathway

    The Hsp70 Ssb serves a dual role in de novo protein folding and ribosome biogenesis; however, the mechanism by which Ssb affects ribosome production is unclear. Here we establish that Ssb is causally linked to...

    Kaivalya Mudholkar, Edith Fitzke, Claudia Prinz, Matthias P. Mayer in Nature Communications (2017)

  5. No Access

    Article

    Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC

    The ribosome-associated complex (RAC) is formed by the JD protein Zuo1 and the unconventional Hsp70 Ssz1. This Review presents recent developments that have increased our understanding of RAC's mechanisms and ...

    Ying Zhang, Irmgard Sinning, Sabine Rospert in Nature Structural & Molecular Biology (2017)

  6. Article

    Open Access

    The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains

    Activation of the heterotrimeric kinase SNF1 via phosphorylation of a specific residue within the α subunit is essential for the release from glucose repression in the yeast Saccharomyces cerevisiae. When glucose...

    Volker Hübscher, Kaivalya Mudholkar, Sabine Rospert in Current Genetics (2017)

  7. Article

    Open Access

    Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain

    Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue...

    Andrea Gumiero, Charlotte Conz, Genís Valentín Gesé, Ying Zhang in Nature Communications (2016)

  8. No Access

    Article

    Am Ende des Tunnels — Ribosomenassoziierte Proteinbiogenesefaktoren

    Ribosome-bound protein biogenesis factors (RPBs) are essential for the early steps of protein biogenesis. A hallmark of RPBs is their ability to bind to the platform surrounding the exit of the ribosomal polyp...

    Ying Zhang, Sachiko Hayashi, Arlette Tais, Vinzenz Bothe, Sabine Rospert in BIOspektrum (2012)

  9. No Access

    Article

    Transcriptional activation of polycomb-repressed genes by ZRF1

    Ubiquitination of histone H2A has been implicated in polycomb-mediated transcriptional silencing, but its precise functions are unclear. Here, the phosphoprotein ZRF1 (zuotin-related factor 1) is shown to be r...

    Holger Richly, Luciana Rocha-Viegas, Joana Domingues Ribeiro, Santiago Demajo in Nature (2010)

  10. Article

    Distinct yet linked: chaperone networks in the eukaryotic cytosol

    The terms chaperone and heat-shock protein are frequently used as synonyms, but this is an oversimplification. Although one subset of chaperones is induced by heat stress, a distinct group fails to respond in ...

    Sabine Rospert, Agnieszka Chacinska in Genome Biology (2006)

  11. No Access

    Article

    The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1

    J-proteins are obligate partners of Hsp70s, forming a ubiquitous class of molecular chaperone machinery. The ribosome-associated Hsp70 of yeast Ssb binds nascent polypeptides as they exit the ribosome. Here we...

    Peggy Huang, Matthias Gautschi, William Walter in Nature Structural & Molecular Biology (2005)

  12. No Access

    Article

    Machinery for protein sorting and assembly in the mitochondrial outer membrane

    Mitochondria contain translocases for the transport of precursor proteins across their outer and inner membranes1,2,3,4,5. It has been assumed that the translocases also mediate the sorting of proteins to their s...

    Nils Wiedemann, Vera Kozjak, Agnieszka Chacinska, Birgit Schönfisch in Nature (2003)

  13. No Access

    Protocol

    Purification of Yeast Mitochondrial Hsp60

    Hsp60 from yeast is a close homolog of bacterial GroEL and located in the matrix of mitochondria. Yeast mitochondrial hsp60 is encoded by an essential gene and its expression is induced two- to threefold upon ...

    Yves Dubaquié, Renate Looser, Sabine Rospert in Chaperonin Protocols (2000)

  14. No Access

    Article

    The biotin-dependent sodium ion pump glutaconyl-CoA decarboxylase from Fusobacterium nucleatum (subsp. nucleatum)

    Membrane preparations of Fusobacterium nucleatum grown on glutamate contain glutaconyl-CoA decarboxylase at a high specific activity (13.8 nkat/mg protein). The enzyme was solubilized with 2% Triton X-100 in 0.5M...

    Birgitta Beatrix, Klaus Bendrat, Sabine Rospert in Archives of Microbiology (1990)