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• W3194368279 abstract "Heat shock proteins of 110 kDa (Hsp110s), a unique class of molecular chaperones, are essential for maintaining protein homeostasis. Hsp110s exhibit a strong chaperone activity preventing protein aggregation (the “holdase” activity) and also function as the major nucleotide-exchange factor (NEF) for Hsp70 chaperones. Hsp110s contain two functional domains: a nucleotide-binding domain (NBD) and substrate-binding domain (SBD). ATP binding is essential for Hsp110 function and results in close contacts between the NBD and SBD. However, the molecular mechanism of this ATP-induced allosteric coupling remains poorly defined. In this study, we carried out biochemical analysis on Msi3, the sole Hsp110 in Candida albicans, to dissect the unique allosteric coupling of Hsp110s using three mutations affecting the domain–domain interface. All the mutations abolished both the in vivo and in vitro functions of Msi3. While the ATP-bound state was disrupted in all mutants, only mutation of the NBD-SBDβ interfaces showed significant ATPase activity, suggesting that the full-length Hsp110s have an ATPase that is mainly suppressed by NBD-SBDβ contacts. Moreover, the high-affinity ATP-binding unexpectedly appears to require these NBD-SBD contacts. Remarkably, the “holdase” activity was largely intact for all mutants tested while NEF activity was mostly compromised, although both activities strictly depended on the ATP-bound state, indicating different requirements for these two activities. Stable peptide substrate binding to Msi3 led to dissociation of the NBD-SBD contacts and compromised interactions with Hsp70. Taken together, our data demonstrate that the exceptionally strong NBD-SBD contacts in Hsp110s dictate the unique allosteric coupling and biochemical activities. Heat shock proteins of 110 kDa (Hsp110s), a unique class of molecular chaperones, are essential for maintaining protein homeostasis. Hsp110s exhibit a strong chaperone activity preventing protein aggregation (the “holdase” activity) and also function as the major nucleotide-exchange factor (NEF) for Hsp70 chaperones. Hsp110s contain two functional domains: a nucleotide-binding domain (NBD) and substrate-binding domain (SBD). ATP binding is essential for Hsp110 function and results in close contacts between the NBD and SBD. However, the molecular mechanism of this ATP-induced allosteric coupling remains poorly defined. In this study, we carried out biochemical analysis on Msi3, the sole Hsp110 in Candida albicans, to dissect the unique allosteric coupling of Hsp110s using three mutations affecting the domain–domain interface. All the mutations abolished both the in vivo and in vitro functions of Msi3. While the ATP-bound state was disrupted in all mutants, only mutation of the NBD-SBDβ interfaces showed significant ATPase activity, suggesting that the full-length Hsp110s have an ATPase that is mainly suppressed by NBD-SBDβ contacts. Moreover, the high-affinity ATP-binding unexpectedly appears to require these NBD-SBD contacts. Remarkably, the “holdase” activity was largely intact for all mutants tested while NEF activity was mostly compromised, although both activities strictly depended on the ATP-bound state, indicating different requirements for these two activities. Stable peptide substrate binding to Msi3 led to dissociation of the NBD-SBD contacts and compromised interactions with Hsp70. Taken together, our data demonstrate that the exceptionally strong NBD-SBD contacts in Hsp110s dictate the unique allosteric coupling and biochemical activities. Heat shock proteins of 110 kDa (Hsp110s) form a unique class of molecular chaperones (1Easton D.P. Kaneko Y. Subjeck J.R. The hsp110 and Grp1 70 stress proteins: Newly recognized relatives of the Hsp70s.Cell Stress Chaperones. 2000; 5: 276-290Crossref PubMed Scopus (240) Google Scholar, 2Lee-Yoon D. Easton D. Murawski M. Burd R. Subjeck J.R. Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein.J. Biol. Chem. 1995; 270: 15725-15733Abstract Full Text Full Text PDF PubMed Scopus (128) Google Scholar, 3Raviol H. Sadlish H. Rodriguez F. Mayer M.P. Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.EMBO J. 2006; 25: 2510-2518Crossref PubMed Scopus (208) Google Scholar, 4Dragovic Z. Broadley S.A. Shomura Y. Bracher A. Hartl F.U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.EMBO J. 2006; 25: 2519-2528Crossref PubMed Scopus (261) Google Scholar, 5Yam A.Y. Albanese V. Lin H.T. Frydman J. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding.J. Biol. Chem. 2005; 280: 41252-41261Abstract Full Text Full Text PDF PubMed Scopus (72) Google Scholar, 6Shaner L. Trott A. Goeckeler J.L. Brodsky J.L. Morano K.A. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.J. Biol. Chem. 2004; 279: 21992-22001Abstract Full Text Full Text PDF PubMed Scopus (74) Google Scholar, 7Liu X.D. Morano K.A. Thiele D.J. The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.J. Biol. Chem. 1999; 274: 26654-26660Abstract Full Text Full Text PDF PubMed Scopus (101) Google Scholar, 8Shaner L. Morano K.A. All in the family: Atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.Cell Stress Chaperones. 2007; 12: 1-8Crossref PubMed Scopus (77) Google Scholar, 9Yakubu U.M. Morano K.A. Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding.Biol. Chem. 2018; 399: 1215-1221Crossref PubMed Scopus (12) Google Scholar). Ubiquitously present in the eukaryotic cytosol, they play an essential role in maintaining cellular protein homeostasis. Through this role, they provide essential protections for eukaryotic organisms against various stress conditions, including many human diseases. Thus, it is paramount to characterize the precise mechanism(s) of their action in maintaining protein homeostasis to understand their protective role against various diseases. As distant homologs of Hsp70s, Hsp110s are both chaperones on their own and cochaperones for Hsp70s. Hsp70s, an essential and universal class of molecular chaperones, play key roles in virtually all known processes in maintaining protein homeostasis (10Bukau B. Weissman J. Horwich A. Molecular chaperones and protein quality control.Cell. 2006; 125: 443-451Abstract Full Text Full Text PDF PubMed Scopus (1171) Google Scholar, 11Mayer M.P. Bukau B. Hsp70 chaperones: Cellular functions and molecular mechanism.Cell Mol. Life Sci. 2005; 62: 670-684Crossref PubMed Scopus (1993) Google Scholar, 12Balchin D. Hayer-Hartl M. Hartl F.U. In vivo aspects of protein folding and quality control.Science. 2016; 353: aac4354Crossref PubMed Scopus (702) Google Scholar, 13Young J.C. Mechanisms of the Hsp70 chaperone system.Biochem. Cell Biol. 2010; 88: 291-300Crossref PubMed Scopus (144) Google Scholar, 14Liu Q. Liang C. Zhou L. Structural and functional analysis of the Hsp70/Hsp40 chaperone system.Protein Sci. 2020; 29: 378-390Crossref PubMed Scopus (33) Google Scholar, 15Fernandez-Fernandez M.R. Valpuesta J.M. Hsp70 chaperone: A master player in protein homeostasis.F1000Res. 2018; 7 (F1000 Faculty Rev-1497)Crossref PubMed Google Scholar, 16Pobre K.F.R. Poet G.J. Hendershot L.M. The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.J. Biol. Chem. 2019; 294: 2098-2108Abstract Full Text Full Text PDF PubMed Scopus (136) Google Scholar, 17Zuiderweg E.R. Hightower L.E. Gestwicki J.E. The remarkable multivalency of the Hsp70 chaperones.Cell Stress Chaperones. 2017; 22: 173-189Crossref PubMed Scopus (75) Google Scholar). Hsp110s, by themselves, have potent chaperone activity in preventing the aggregation of denatured proteins, the “holdase” activity (18Oh H.J. Chen X. Subjeck J.R. Hsp110 protects heat-denatured proteins and confers cellular thermoresistance.J. Biol. Chem. 1997; 272: 31636-31640Abstract Full Text Full Text PDF PubMed Scopus (171) Google Scholar, 19Goeckeler J.L. Stephens A. Lee P. Caplan A.J. Brodsky J.L. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity.Mol. Biol. Cell. 2002; 13: 2760-2770Crossref PubMed Scopus (69) Google Scholar, 20Mattoo R.U. Sharma S.K. Priya S. Finka A. Goloubinoff P. Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.J. Biol. Chem. 2013; 288: 21399-21411Abstract Full Text Full Text PDF PubMed Scopus (108) Google Scholar, 21Taguchi Y.V. Gorenberg E.L. Nagy M. Thrasher D. Fenton W.A. Volpicelli-Daley L. Horwich A.L. Chandra S.S. Hsp110 mitigates alpha-synuclein pathology in vivo.Proc. Natl. Acad. Sci. U. S. A. 2019; 116: 24310-24316Crossref PubMed Scopus (24) Google Scholar). However, they lack the hallmark activity of Hsp70s in assisting protein folding directly. As cochaperones, Hsp110s have been shown to function as the major nucleotide-exchange factors (NEFs) for cytosolic Hsp70s, facilitating the exchange of ADP for ATP in Hsp70s after ATP hydrolysis (3Raviol H. Sadlish H. Rodriguez F. Mayer M.P. Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.EMBO J. 2006; 25: 2510-2518Crossref PubMed Scopus (208) Google Scholar, 4Dragovic Z. Broadley S.A. Shomura Y. Bracher A. Hartl F.U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.EMBO J. 2006; 25: 2519-2528Crossref PubMed Scopus (261) Google Scholar, 9Yakubu U.M. Morano K.A. Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding.Biol. Chem. 2018; 399: 1215-1221Crossref PubMed Scopus (12) Google Scholar, 22Andreasson C. Fiaux J. Rampelt H. Mayer M.P. Bukau B. Hsp110 is a nucleotide-activated exchange factor for Hsp70.J. Biol. Chem. 2008; 283: 8877-8884Abstract Full Text Full Text PDF PubMed Scopus (112) Google Scholar, 23Bracher A. Verghese J. The nucleotide exchange factors of Hsp70 molecular chaperones.Front. Mol. Biosci. 2015; 2: 10Crossref PubMed Scopus (126) Google Scholar). Various studies have demonstrated that Hsp110s participate in almost all the processes that are associated with cytosolic Hsp70s including de novo protein folding and refolding under stress, protein transportation into the endoplasmic reticulum, solubilizing protein aggregates, and protein degradation (1Easton D.P. Kaneko Y. Subjeck J.R. The hsp110 and Grp1 70 stress proteins: Newly recognized relatives of the Hsp70s.Cell Stress Chaperones. 2000; 5: 276-290Crossref PubMed Scopus (240) Google Scholar, 5Yam A.Y. Albanese V. Lin H.T. Frydman J. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding.J. Biol. Chem. 2005; 280: 41252-41261Abstract Full Text Full Text PDF PubMed Scopus (72) Google Scholar, 7Liu X.D. Morano K.A. Thiele D.J. The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.J. Biol. Chem. 1999; 274: 26654-26660Abstract Full Text Full Text PDF PubMed Scopus (101) Google Scholar, 8Shaner L. Morano K.A. All in the family: Atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.Cell Stress Chaperones. 2007; 12: 1-8Crossref PubMed Scopus (77) Google Scholar, 9Yakubu U.M. Morano K.A. Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding.Biol. Chem. 2018; 399: 1215-1221Crossref PubMed Scopus (12) Google Scholar, 18Oh H.J. Chen X. Subjeck J.R. Hsp110 protects heat-denatured proteins and confers cellular thermoresistance.J. Biol. Chem. 1997; 272: 31636-31640Abstract Full Text Full Text PDF PubMed Scopus (171) Google Scholar, 19Goeckeler J.L. Stephens A. Lee P. Caplan A.J. Brodsky J.L. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity.Mol. Biol. Cell. 2002; 13: 2760-2770Crossref PubMed Scopus (69) Google Scholar, 20Mattoo R.U. Sharma S.K. Priya S. Finka A. Goloubinoff P. Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.J. Biol. Chem. 2013; 288: 21399-21411Abstract Full Text Full Text PDF PubMed Scopus (108) Google Scholar, 24Shaner L. Wegele H. Buchner J. Morano K.A. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb.J. Biol. Chem. 2005; 280: 41262-41269Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar, 25Albanese V. Yam A.Y. Baughman J. Parnot C. Frydman J. Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells.Cell. 2006; 124: 75-88Abstract Full Text Full Text PDF PubMed Scopus (194) Google Scholar, 26Fan Q. Park K.W. Du Z. Morano K.A. Li L. The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.Genetics. 2007; 177: 1583-1593Crossref PubMed Scopus (73) Google Scholar, 27Hrizo S.L. Gusarova V. Habiel D.M. Goeckeler J.L. 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Scholz S.R. Morimoto R.I. Bukau B. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation.EMBO J. 2012; 31: 4221-4235Crossref PubMed Scopus (213) Google Scholar, 32Mandal A.K. Gibney P.A. Nillegoda N.B. Theodoraki M.A. Caplan A.J. Morano K.A. Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system.Mol. Biol. Cell. 2010; 21: 1439-1448Crossref PubMed Google Scholar, 33Ravindran M.S. Bagchi P. Inoue T. Tsai B. A non-enveloped virus hijacks host disaggregation machinery to translocate across the endoplasmic reticulum membrane.PLoS Pathog. 2015; 11e1005086Crossref PubMed Scopus (37) Google Scholar, 34Gao X. Carroni M. Nussbaum-Krammer C. Mogk A. Nillegoda N.B. Szlachcic A. Guilbride D.L. Saibil H.R. Mayer M.P. Bukau B. Human Hsp70 disaggregase reverses Parkinson's-linked alpha-synuclein amyloid fibrils.Mol. Cell. 2015; 59: 781-793Abstract Full Text Full Text PDF PubMed Scopus (218) Google Scholar, 35Kandasamy G. Andreasson C. Hsp70-Hsp110 chaperones deliver ubiquitin-dependent and -independent substrates to the 26S proteasome for proteolysis in yeast.J. Cell Sci. 2018; 131jcs210948Crossref PubMed Scopus (23) Google Scholar, 36Moran C. Kinsella G.K. Zhang Z.R. Perrett S. Jones G.W. Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.G3 (Bethesda). 2013; 3: 1409-1418Crossref PubMed Scopus (13) Google Scholar, 37O'Driscoll J. Clare D. Saibil H. Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.J. Cell Biol. 2015; 211: 145-158Crossref PubMed Scopus (21) Google Scholar, 38Hatayama T. Yasuda K. Association of HSP105 with HSC70 in high molecular mass complexes in mouse FM3A cells.Biochem. Biophys. Res. Commun. 1998; 248: 395-401Crossref PubMed Scopus (46) Google Scholar, 39Wang X.Y. Chen X. Oh H.J. Repasky E. Kazim L. Subjeck J. Characterization of native interaction of hsp110 with hsp25 and hsc70.FEBS Lett. 2000; 465: 98-102Crossref PubMed Scopus (44) Google Scholar). However, the functional roles of Hsp110s beyond NEFs remain a mystery. The unique biochemical properties of Hsp110s dictate their special chaperone activities. As homologs, Hsp110s share the same domain organization as Hsp70s (1Easton D.P. Kaneko Y. Subjeck J.R. The hsp110 and Grp1 70 stress proteins: Newly recognized relatives of the Hsp70s.Cell Stress Chaperones. 2000; 5: 276-290Crossref PubMed Scopus (240) Google Scholar, 8Shaner L. Morano K.A. All in the family: Atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.Cell Stress Chaperones. 2007; 12: 1-8Crossref PubMed Scopus (77) Google Scholar, 9Yakubu U.M. Morano K.A. Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding.Biol. Chem. 2018; 399: 1215-1221Crossref PubMed Scopus (12) Google Scholar, 14Liu Q. Liang C. Zhou L. Structural and functional analysis of the Hsp70/Hsp40 chaperone system.Protein Sci. 2020; 29: 378-390Crossref PubMed Scopus (33) Google Scholar, 40Liu Q. Hendrickson W.A. Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1.Cell. 2007; 131: 106-120Abstract Full Text Full Text PDF PubMed Scopus (190) Google Scholar). Both Hsp110s and Hsp70s have two functional domains: a nucleotide-binding domain (NBD) at the N-terminus and a substrate-binding domain (SBD) at the C-terminus. The SBD is further divided into SBDβ and SBDα. Connecting these two functional domains is a short interdomain linker. Hsp110s are larger in size due to an insertion in the SBDβ and a C-terminal extension beyond the SBDα. A recent study suggested a novel substrate-binding site in the C-terminal extension region of metazoan Hsp110s but not yeast Hsp110s (41Yakubu U.M. Morano K.A. Suppression of aggregate and amyloid formation by a novel intrinsically disordered region in metazoan Hsp110 chaperones.J. Biol. Chem. 2021; : 100567Abstract Full Text Full Text PDF PubMed Scopus (2) Google Scholar). However, it is puzzling that both these extra segments are dispensable for function (6Shaner L. Trott A. Goeckeler J.L. Brodsky J.L. Morano K.A. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.J. Biol. Chem. 2004; 279: 21992-22001Abstract Full Text Full Text PDF PubMed Scopus (74) Google Scholar, 40Liu Q. Hendrickson W.A. Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1.Cell. 2007; 131: 106-120Abstract Full Text Full Text PDF PubMed Scopus (190) Google Scholar, 42Oh H.J. Easton D. Murawski M. Kaneko Y. Subjeck J.R. The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions.J. Biol. Chem. 1999; 274: 15712-15718Abstract Full Text Full Text PDF PubMed Scopus (120) Google Scholar). The biochemical properties and structures of Hsp70s are well studied. For Hsp70s, each functional domain has an essential intrinsic activity (10Bukau B. Weissman J. Horwich A. Molecular chaperones and protein quality control.Cell. 2006; 125: 443-451Abstract Full Text Full Text PDF PubMed Scopus (1171) Google Scholar, 11Mayer M.P. Bukau B. Hsp70 chaperones: Cellular functions and molecular mechanism.Cell Mol. Life Sci. 2005; 62: 670-684Crossref PubMed Scopus (1993) Google Scholar, 13Young J.C. Mechanisms of the Hsp70 chaperone system.Biochem. Cell Biol. 2010; 88: 291-300Crossref PubMed Scopus (144) Google Scholar, 14Liu Q. Liang C. Zhou L. Structural and functional analysis of the Hsp70/Hsp40 chaperone system.Protein Sci. 2020; 29: 378-390Crossref PubMed Scopus (33) Google Scholar, 43Mayer M.P. Gierasch L.M. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones.J. Biol. Chem. 2019; 294: 2085-2097Abstract Full Text Full Text PDF PubMed Scopus (125) Google Scholar, 44Bukau B. Horwich A.L. The Hsp70 and Hsp60 chaperone machines.Cell. 1998; 92: 351-366Abstract Full Text Full Text PDF PubMed Scopus (2397) Google Scholar). The NBD binds ATP or ADP and hydrolyzes bound ATP to ADP, i.e., the NBD has an ATPase activity. The SBD binds hydrophobic segments of polypeptides in extended conformation, normally only found in unfolded proteins. As there is little contact between the two domains in the ADP-bound and nucleotide-free (apo) states, the isolated SBD structures represent these states (45Buchberger A. Theyssen H. Schroder H. McCarty J.S. Virgallita G. Milkereit P. Reinstein J. Bukau B. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.J. Biol. 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Peptide binding and release by proteins implicated as catalysts of protein assembly.Science. 1989; 245: 385-390Crossref PubMed Scopus (572) Google Scholar). This allosteric coupling is crucial for the chaperone activity by ensuring that the energy from ATP hydrolysis is efficiently used for regulating peptide substrate binding (14Liu Q. Liang C. Zhou L. Structural and functional analysis of the Hsp70/Hsp40 chaperone system.Protein Sci. 2020; 29: 378-390Crossref PubMed Scopus (33) Google Scholar, 43Mayer M.P. Gierasch L.M. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones.J. Biol. Chem. 2019; 294: 2085-2097Abstract Full Text Full Text PDF PubMed Scopus (125) Google Scholar, 45Buchberger A. Theyssen H. Schroder H. McCarty J.S. Virgallita G. Milkereit P. Reinstein J. Bukau B. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.J. Biol. 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Fitzke E. Wolfle T. Fischer T. Rospert S. Sinning I. Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.Nat. Commun. 2016; 7: 13563Crossref PubMed Scopus (31) Google Scholar). In contrast, limited biochemical and structural information is available for Hsp110s. Although Hsp110s have the two functional domains such as Hsp70s, it has been enigmatic whether Hsp110s have similar intrinsic activities and allosteric coupling. The ATP binding is essential for the “holdase” activity and NEF activity of Hsp110s (6Shaner L. Trott A. Goeckeler J.L. Brodsky J.L. Morano K.A. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.J. Biol. Chem. 2004; 279: 21992-22001Abstract Full Text Full Text PDF PubMed Scopus (74) Google Scholar, 9Yakubu U.M. Morano K.A. Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding.Biol. Chem. 2018; 399: 1215-1221Crossref PubMed Scopus (12) Google Scholar, 22Andreasson C. Fiaux J. Rampelt H. Mayer M.P. Bukau B. Hsp110 is a nucleotide-activated exchange factor for Hsp70.J. Biol. Chem. 2008; 283: 8877-8884Abstract Full Text Full Text PDF PubMed Scopus (112) Google Scholar, 23Bracher A. Verghese J. The nucleotide exchange factors of Hsp70 molecular chaperones.Front. Mol. Biosci. 2015; 2: 10Crossref PubMed Scopus (126) Google Scholar, 56Polier S. Dragovic Z. Hartl F.U. Bracher A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.Cell. 2008; 133: 1068-1079Abstract Full Text Full Text PDF PubMed Scopus (199) Google Scholar); however, it has been under debate whether Hsp110s have an active ATPase activity (3Raviol H. Sadlish H. Rodriguez F. Mayer M.P. Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.EMBO J. 2006; 25: 2510-2518Crossref PubMed Scopus (208) Google Scholar, 20Mattoo R.U. Sharma S.K. Priya S. Finka A. Goloubinoff P. Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.J. Biol. Chem. 2013; 288: 21399-21411Abstract Full Text Full Text PDF PubMed Scopus (108) Google Scholar, 24Shaner L. Wegele H. Buchner J. Morano K.A. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb.J. Biol. Chem. 2005; 280: 41262-41269Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar, 56Polier S. Dragovic Z. Hartl F.U. Bracher A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.Cell. 2008; 133: 1068-1079Abstract Full Text Full Text PDF PubMed Scopus (199) Google Scholar, 57Yamagishi N. Ishihara K. Hatayama T. 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• W3194368279 date "2021-09-01" @default.
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• W3194368279 title "Interdomain interactions dictate the function of the Candida albicans Hsp110 protein Msi3" @default.
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