Uncoating ATPase is a member of the 70 kilodalton family of stress proteins

Academic Article

Abstract

  • The synthetic peptide, VGIDLGTTYSC, derived from the heat shock-induced genes human hsp70, Drosophila hsp70, S. cerevisiae YG100, and E. coli dnaK, elicited antibodies that recognized two constitutive proteins in bovine extracts. One of these proteins, 71 kd, has previously been identified as uncoating ATPase, an enzyme that releases clathrin from coated vesicies. This immunological data complemented the result that uncoating ATPase was indistinguishable from the constitutive mammalian 71 kd stress protein by either partial proteolytic mapping or two-dimensional gel analysis. In addition, affinity-purified uncoating ATPase antibodies recognize proteins in yeast identified as the gene products of the heat shock or heat shock cognate genes YG100 and YG102. The results show that uncoating ATPase is a member of the 70 kd heat shock protein family. © 1986.
  • Published In

  • Cell  Journal
  • Digital Object Identifier (doi)

    Author List

  • Chappell TG; Welch WJ; Schlossman DM; Palter KB; Schlesinger MJ; Rothman JE
  • Start Page

  • 3
  • End Page

  • 13
  • Volume

  • 45
  • Issue

  • 1