FOG02831
EOG8X69Q9

sce:HSP104

Genes: 34

SGD Description
Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation


PomBase Description
heat shock protein Hsp104 (predicted)


AspGD Description
Ortholog(s) have ATPase activity, misfolded protein binding activity, role in cellular response to misfolded protein, protein refolding, protein unfolding and cytosol, nuclear envelope localization


References

Sanchez Y, et al. (1990 Jun 1). HSP104 required for induced thermotolerance.

Parsell DA, et al. (1991 Sep 19). Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.

Sanchez Y, et al. (1992 Jun). Hsp104 is required for tolerance to many forms of stress.

Sanchez Y, et al. (1993 Oct). Genetic evidence for a functional relationship between Hsp104 and Hsp70.

Parsell DA, et al. (1994 Dec 1). Protein disaggregation mediated by heat-shock protein Hsp104.

Parsell DA, et al. (1994 Feb 11). Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes.

Chernoff YO, et al. (1995 May 12). Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].

Lindquist S, et al. (1996 May 28). Heat-shock protein 104 expression is sufficient for thermotolerance in yeast.

Schirmer EC, et al. (1998). Purification and properties of Hsp104 from yeast.

Glover JR, et al. (1998 Jul 10). Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Fujita K, et al. (1998 Jul 30). Hsp104 responds to heat and oxidative stress with different intracellular localization in Saccharomyces cerevisiae.

Schirmer EC, et al. (1998 Jun 19). The ATPase activity of Hsp104, effects of environmental conditions and mutations.

Kawai R, et al. (1999 Mar). Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy.

Moriyama H, et al. (2000 Dec). [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.

Sondheimer N, et al. (2000 Jan). Rnq1: an epigenetic modifier of protein function in yeast.

Schirmer EC, et al. (2001 Jan 30). Subunit interactions influence the biochemical and biological properties of Hsp104.

Jung G, et al. (2001 Jul). Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions.

Ferreira PC, et al. (2001 Jun). The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation.

Abbas-Terki T, et al. (2001 Nov). Hsp104 interacts with Hsp90 cochaperones in respiring yeast.

Cashikar AG, et al. (2002 Apr). Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein.

Grably MR, et al. (2002 Apr). HSF and Msn2/4p can exclusively or cooperatively activate the yeast HSP104 gene.

Ness F, et al. (2002 Aug). Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast.

Hattendorf DA, et al. (2002 Jan 15). Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.

Jung G, et al. (2002 Jul 23). Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance.

Hattendorf DA, et al. (2002 Mar 5). Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.

Kryndushkin DS, et al. (2003 Dec 5). Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.

Hitchcock AL, et al. (2003 Oct 28). A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.

Seppä L, et al. (2004 Apr). Upregulation of the Hsp104 chaperone at physiological temperature during recovery from thermal insult.

Grimminger V, et al. (2004 Feb 27). The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104.

Lum R, et al. (2004 Jul 9). Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.

Shorter J, et al. (2004 Jun 18). Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers.

Schirmer EC, et al. (2004 May). Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.

Cashikar AG, et al. (2005 Jun 24). A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.

Haslbeck M, et al. (2005 Jun 24). Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104.

Bösl B, et al. (2005 Nov 18). Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.

Shorter J, et al. (2006 Aug 4). Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.

Narayanan S, et al. (2006 May). Yeast prion-protein, sup35, fibril formation proceeds by addition and substraction of oligomers.

Wendler P, et al. (2007 Dec 28). Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.

Doyle SM, et al. (2007 Feb). Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.

Satpute-Krishnan P, et al. (2007 Feb). Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance.

Schaupp A, et al. (2007 Jul 20). Processing of proteins by the molecular chaperone Hsp104.

Kurahashi H, et al. (2007 Mar). Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation.

Tessarz P, et al. (2008 Apr). Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation.

Kaganovich D, et al. (2008 Aug 28). Misfolded proteins partition between two distinct quality control compartments.

Mackay RG, et al. (2008 Feb 19). The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly.

Tkach JM, et al. (2008 Jan). Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells.

Colabardini AC, et al. (2010 Dec). Involvement of the Aspergillus nidulans protein kinase C with farnesol tolerance is related to the unfolded protein response.

Starita LM, et al. (2012 Jan). Sites of ubiquitin attachment in Saccharomyces cerevisiae.

Van Damme P, et al. (2012 Jul 31). N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

Egan MJ, et al. (2015 Apr 14). Cytoplasmic dynein is required for the spatial organization of protein aggregates in filamentous fungi.

Mitochondrial localization predictions
Predotar	TargetP	MitoProt
Raw data
Phobius transmembrane predictions 0 genes with posterior transmembrane prediction > 50%

FOG02832
EOG8X69Q9

sce:HSP78

Genes: 34

SGD Description
Oligomeric mitochondrial matrix chaperone; cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates


PomBase Description
mitochondrial heatshock protein Hsp78 (predicted)


AspGD Description
Has domain(s) with predicted ATP binding, nucleoside-triphosphatase activity, nucleotide binding activity


References

Leonhardt SA, et al. (1993 Oct). HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.

Moczko M, et al. (1995 Dec 8). The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function.

Schmitt M, et al. (1995 Jul 17). Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70.

Schmitt M, et al. (1996 Sep). The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.

Krzewska J, et al. (2001 Dec 7). Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein.

Krzewska J, et al. (2001 Jan 26). Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding.

Germaniuk A, et al. (2002 Aug 2). A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase.

Rottgers K, et al. (2002 Nov 29). The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix.

Sickmann A, et al. (2003 Nov 11). The proteome of Saccharomyces cerevisiae mitochondria.

Seppä L, et al. (2005 Dec). Regulation and recovery of functions of Saccharomyces cerevisiae chaperone BiP/Kar2p after thermal insult.

Lewandowska A, et al. (2006 Feb). Hsp78 chaperone functions in restoration of mitochondrial network following heat stress.

von Janowsky B, et al. (2006 Mar 31). The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress.

Wendland J, et al. (2011 Dec). Genome evolution in the eremothecium clade of the Saccharomyces complex revealed by comparative genomics.

Coradetti ST, et al. (2013 Aug). Analysis of a conserved cellulase transcriptional regulator reveals inducer-independent production of cellulolytic enzymes in Neurospora crassa.

Mitochondrial localization predictions
Predotar	TargetP	MitoProt
Raw data
Phobius transmembrane predictions 1 genes with posterior transmembrane prediction > 50%