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Literature summary for 5.6.1.7 extracted from

  • Hawkins, T.A.; Haramis, A.; Etard, C.; Prodromou, C.; Vaughan, C.K.; Ashworth, R.; Ray, S.; Behra, M.; Holder, N.; Talbot, W.S.; Pearl, L.H.; Strahle, U.; Wilson, S.W.
    The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis (2008), Development, 135, 1147-1156.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
full-length u45 mutant and wild-type hsp90a are amplified by RT-PCR, cloned into the the TOPO vector and subcloned by PCR into pCS2myc+ Danio rerio

Protein Variants

Protein Variants Comment Organism
slou45 the ATPase activity of Hsp90 is abrogated by the slou45 mutation Danio rerio

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a folded polypeptide Danio rerio
-
 ADP + phosphate + an unfolded polypeptide
-
 ir

Organism

Organism UniProt Comment Textmining
Danio rerio
-
-
-

Purification (Commentary)

Purification (Comment) Organism
protein is extracted by homogenisation of deyolked embryos Danio rerio

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
 Danio rerio
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide
-
 Danio rerio ADP + phosphate + an unfolded polypeptide
-
 ir

Synonyms

Synonyms Comment Organism
Hsp90a
-
 Danio rerio