| Pathway of Hsp70 interactions at the ribosome. | Pathway of Hsp70 interactions at the ribosome.
Lee K, Ziegelhoffer T, Delewski W, Berger SE, Sabat G, Craig EA., Free PMC Article | 10/23/2021 |
| Cooperativity between the Ribosome-Associated Chaperone Ssb/RAC and the Ubiquitin Ligase Ltn1 in Ubiquitination of Nascent Polypeptides. | Cooperativity between the Ribosome-Associated Chaperone Ssb/RAC and the Ubiquitin Ligase Ltn1 in Ubiquitination of Nascent Polypeptides.
Ghosh A, Shcherbik N., Free PMC Article | 03/20/2021 |
| Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation. | Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.
Nicklow EE, Sevier CS., Free PMC Article | 09/19/2020 |
| A positively charged region in the alpha-helical lid domain of SSB is identified. It is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation. | Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.
Gumiero A, Conz C, Gesé GV, Zhang Y, Weyer FA, Lapouge K, Kappes J, von Plehwe U, Schermann G, Fitzke E, Wölfle T, Fischer T, Rospert S, Sinning I., Free PMC Article | 09/29/2018 |
| Data show that the absence of either Ssb1/2 or Sch9 causes enhanced ribosome aggregation. | The Hsp70 homolog Ssb affects ribosome biogenesis via the TORC1-Sch9 signaling pathway.
Mudholkar K, Fitzke E, Prinz C, Mayer MP, Rospert S., Free PMC Article | 03/10/2018 |
| Study reveals molecular features of chaperone action during translation in eukaryotes by providing proteome-wide Ssb (two isoforms Ssb1 and Ssb2) interaction profiles with nascent chains at near-codon resolution. The Ssb interactome is broader than previously thought and includes nascent mitochondrial and endoplasmic reticulum- (ER) translocated proteins. | Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding.
Döring K, Ahmed N, Riemer T, Suresh HG, Vainshtein Y, Habich M, Riemer J, Mayer MP, O'Brien EP, Kramer G, Bukau B., Free PMC Article | 08/5/2017 |
| the ribosome-associated Hsp70 Ssb is redistributed away from Sup35 prion aggregates to the nascent chains, leading to an array of aggregation phenotypes that can mimic both overexpression and deletion of Ssb. | Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.
Keefer KM, True HL., Free PMC Article | 05/13/2017 |
| Studied deletions of two major chaperone proteins, SSA1 and SSB1, from the HSP70 chaperone network in Sacchromyces cerevisiae. | Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in Saccharomyces cerevisiae.
Jarnuczak AF, Eyers CE, Schwartz JM, Grant CM, Hubbard SJ., Free PMC Article | 06/28/2016 |
| Study finds that SSB (i.e. closely related isoforms Ssb1 and Ssb2) binds to a subset of nascent polypeptides whose intrinsic properties and slow translation rates hinder efficient cotranslational folding. | The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.
Willmund F, del Alamo M, Pechmann S, Chen T, Albanèse V, Dammer EB, Peng J, Frydman J., Free PMC Article | 03/23/2013 |
| The ribosome-bound chaperone system consisting of the ribosome-associated complex (RAC) and the Hsp70 homologs SSB1 and SSB2 are required to stabilize translationally repressed ribosome-polylysine protein complexes. | Ribosome-associated complex and Ssb are required for translational repression induced by polylysine segments within nascent chains.
Chiabudini M, Conz C, Reckmann F, Rospert S., Free PMC Article | 01/26/2013 |
| Zuo1 and Ssz1 together with the Hsp70 homolog Ssb1/2 form a functional triad involved in translation and early polypeptide folding processes. | Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex.
Conz C, Otto H, Peisker K, Gautschi M, Wölfle T, Mayer MP, Rospert S. | 01/21/2010 |
| ssb and zuo1 have a role in cation influx in Saccharomyces cerevisiae membranes | Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides.
Kim SY, Craig EA., Free PMC Article | 01/21/2010 |
| A plausible role of the Ssb1 chaperone is to stabilize genetic networks, thus making them more tolerant to malfunctioning of their constituents. | Why molecular chaperones buffer mutational damage: a case study with a yeast Hsp40/70 system.
Bobula J, Tomala K, Jez E, Wloch DM, Borts RH, Korona R., Free PMC Article | 01/21/2010 |
| Jjj1, when overexpressed, is able to partially substitute for the Zuo1:Ssb chaperone machinery by recruiting Ssa to the ribosome, facilitating its interaction with nascent polypeptide chains | The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis.
Meyer AE, Hung NJ, Yang P, Johnson AW, Craig EA., Free PMC Article | 01/21/2010 |
| Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb | The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb.
Shaner L, Wegele H, Buchner J, Morano KA. | 01/21/2010 |
| Results suggest that RAC and Ssb1/2p are crucial in maintaining translational fidelity beyond their postulated role as chaperones for nascent polypeptides. | The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae.
Rakwalska M, Rospert S., Free PMC Article | 01/21/2010 |
| SSB/SSE and SSA/SSE transiently associate with newly synthesized polypeptides with different kinetics | Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding.
Yam AY, Albanèse V, Lin HT, Frydman J. | 01/21/2010 |