Fungal protein found in Saccharomyces cerevisiae S288c
Heat shock protein 104
Identifiers
Organism
Saccharomyces cerevisiae
Symbol
HSP104
Entrez
850633
PDB
5VJH
RefSeq (mRNA)
1NM_001181846.1
RefSeq (Prot)
NP_013074.
UniProt
P31539
Other data
Chromosome
XII: 0.09 - 0.09 Mb
Search for
Structures
Swiss-model
Domains
InterPro
Hsp104 is a heat-shock protein. It is known to reverse toxicity of mutant α-synuclein, TDP-43, FUS, and TAF15 in yeast cells.[1] Conserved in prokaryotes (ClpB), fungi, plants and as well as animal mitochondria, there is yet to see hsp104 in multicellular animals. Hsp104 is classified as a. AAA+ ATPases and a subgroup of Hsp100/Clp, because of the usage of Atp hydrolysis for structural modulation of other proteins.[2] Hsp104 is not needed for normal cell growth but when exposed to stress there is an increase amount. Removing the aggregates without the hsp104 is insufficient there highlighting the importance of this heat shock protein and its interactions.[3]
^"Yeast Chaperone Melts Protein Aggregates". Alzforum.org. Retrieved September 12, 2016.
^Romanova NV, Chernoff YO (2009). "Hsp104 and prion propagation". Protein and Peptide Letters. 16 (6): 598–605. doi:10.2174/092986609788490078. PMC 2791106. PMID 19519517.
^Cite error: The named reference Bösl_2006 was invoked but never defined (see the help page).
Hsp104 is a heat-shock protein. It is known to reverse toxicity of mutant α-synuclein, TDP-43, FUS, and TAF15 in yeast cells. Conserved in prokaryotes...
to a prion negative phenotype). This is the result of inhibition of the Hsp104 chaperone protein known to play an important role in prion fiber fragmentation...
[PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104". J Biol Chem. 278 (49): 49636–43. doi:10.1074/jbc.M307996200. PMID 14507919...
[PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104". The Journal of Biological Chemistry. 278 (49): 49636–43. doi:10.1074/jbc...
of steroid receptors and transcription factors 100 kDa ClpB, ClpA, ClpX Hsp104 (CLPB) Unfolding of insoluble protein aggregates; co-factor of DnaK/Hsp70...
refolding to the prion configuration is assisted by chaperone proteins such as Hsp104. All known prions induce the formation of an amyloid fold, in which the...
coli and Ssa1-Ydj1/Sis1-Sse1/Fe1 in yeast) and Hsp100 (ClpB in E. coli and Hsp104 in yeast) chaperones for protein disaggregation and refolding. Hsp70 interacts...
heritable forms of protein. Because of the action of chaperones, especially Hsp104, proteins that code for [PSI+] and [URE3] can convert from non-prion to...
thermotolerance in Saccharomyces cerevisiae without heat shock protein hsp104 and in the absence of protein synthesis". FEBS Letters. 288 (1–2): 86–90...
have functions other than proteolysis. ClpB (human CLPB "Hsp78", yeast Hsp104) break up insoluble protein aggregates in conjunction with DnaK/Hsp70. They...
potassium transport mutant: identification of a mammalian member of the Clp/HSP104 family". Gene. 152 (2): 157–63. doi:10.1016/0378-1119(94)00697-Q. PMID 7835694...
Nups. Several of these inducible genes, including GAL1, INO1, TSA2, and HSP104 contain gene recruitment sequences (GRSs) found in the promoter, which are...
the disaggregase chaperone, AAA protein HSP104, localizes to the IPOD. It is yet to be determined if HSP104 functions in the IPOD or is simply sequestered...
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