| Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1. | Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1.
Kumar V, Peter JJ, Sagar A, Ray A, Jha MP, Rebeaud ME, Tiwari S, Goloubinoff P, Ashish F, Mapa K. | 10/24/2020 |
| The Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes. | Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product.
Sugiyama T, Nobuta R, Ando K, Matsuki Y, Inada T. | 09/23/2017 |
| A key role for Sse1 (Hsp110), in cooperation with Hsp104, in regulating the length and assembly state of [PSI+] prion fibrils in vivo. | Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.
O'Driscoll J, Clare D, Saibil H., Free PMC Article | 02/6/2016 |
| cytosolic Hsp70 interacts with up to three types of nucleotide exchange factors (NEFs) homologous to human counterparts: Sse1/Sse2 (Heat shock protein 110 (Hsp110)), Fes1 (HspBP1), and Snl1 (Bag-1). | Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.
Abrams JL, Verghese J, Gibney PA, Morano KA., Free PMC Article | 06/28/2014 |
| 13 novel mutations in Sse1 have varying effects on both the ability of S. cerevisiae to propagate the [PSI+] prion and also to grow at increased temperatures. | Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.
Moran C, Kinsella GK, Zhang ZR, Perrett S, Jones GW., Free PMC Article | 03/22/2014 |
| Studies indicate that Sse1 and Sse2 chaperones define the Hsp110 subclass of the Hsp70 chaperones. | The control of spindle length by Hsp70 and Hsp110 molecular chaperones.
Makhnevych T, Houry WA. | 06/1/2013 |
| The role of Hsp110 Sse1 as a nucleotide exchange factor for the Hsp70 chaperones Ssa1/Ssa2 is required for maintaining proper distribution of kinesin-5 motors within the spindle, which is subsequently required for bipolar spindle assembly in S phase. | Hsp110 is required for spindle length control.
Makhnevych T, Wong P, Pogoutse O, Vizeacoumar FJ, Greenblatt JF, Emili A, Houry WA., Free PMC Article | 11/17/2012 |
| Findings support a model in which Hsp110 chaperones control the fate of some client proteins by influencing the decision to fold or degrade as dictated by the Hsp70-Hsp90 chaperone environment. | Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system.
Mandal AK, Gibney PA, Nillegoda NB, Theodoraki MA, Caplan AJ, Morano KA., Free PMC Article | 08/23/2010 |
| compare Grp170 Lhs1 with Hsp110 Sse1 and find that residues important for Sse1 nucleotide exchange factor (NEF) activity are conserved in Lhs1 and that mutations in these residues in Lhs1 compromise NEF activity | The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.
Andréasson C, Rampelt H, Fiaux J, Druffel-Augustin S, Bukau B., Free PMC Article | 05/10/2010 |
| Sse1 exploits a Bag-1-like mechanism to catalyze nucleotide release, which involves opening of the Ssa1 NBD by tilting lobe II. Hsp110 proteins use a unique binding mode to catalyze nucleotide release from Hsp70s by a functionally convergent mechanism | Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity.
Andréasson C, Fiaux J, Rampelt H, Druffel-Augustin S, Bukau B., Free PMC Article | 01/21/2010 |
| mechanistic model wherein Sse1 functionally partners with Hsp90 as an Hsp70 nucleotide exchange factor to promote client protein maturation and interaction with downstream effectors | The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis.
Shaner L, Gibney PA, Morano KA., Free PMC Article | 01/21/2010 |
| The structure of an Hsp110:Hsc70 nucleotide exchange complex, is reported. | Structure of the Hsp110:Hsc70 nucleotide exchange machine.
Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, Gimenez LE, Jin S, Taylor AB, Demeler B, Morano KA, Hart PJ, Valpuesta JM, Lafer EM, Sousa R., Free PMC Article | 01/21/2010 |
| Data suggest that Sse1p does not employ the nucleotide-dependent allostery and peptide-binding mode of canonical Hsp70s, and that direct interactions of substrate with Sse1p may support Hsp70-assisted protein folding in a cooperative process. | Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
Polier S, Dragovic Z, Hartl FU, Bracher A. | 01/21/2010 |
| NEF activity of Sse1 requires nucleotide binding and let us propose a new model for Hsp110 function. | Hsp110 is a nucleotide-activated exchange factor for Hsp70.
Andréasson C, Fiaux J, Rampelt H, Mayer MP, Bukau B. | 01/21/2010 |
| Data suggest that Sse1(ATP) may be an evolutionary vestige of the Hsp70(ATP) state, and an analysis of 64 mutant variants in Sse1 and three Hsp70 homologs supports this hypothesis. | Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1.
Liu Q, Hendrickson WA., Free PMC Article | 01/21/2010 |
| Overproduction of the Sse1 chaperone dramatically enhanced [PSI+] formation whereas deletion of SSE1 severely inhibited it. | The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.
Fan Q, Park KW, Du Z, Morano KA, Li L., Free PMC Article | 01/21/2010 |
| Data show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3] prion propagation. | Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.
Kryndushkin D, Wickner RB., 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 |
| The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A signaling. | The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae.
Trott A, Shaner L, Morano KA., 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 |