The ATPase core of a clathrin uncoating protein

J Biol Chem. 1987 Jan 15;262(2):746-51.

Abstract

Chymotryptic digestion of bovine brain uncoating ATPase produced a 60-kDa fragment that was subsequently proteolyzed to 44 kDa. Loss of clathrin cage uncoating activity paralleled the conversion of the intact 70-kDa enzyme to the 60-kDa fragment, while clathrin binding activity was lost as the 60-kDa fragment was degraded to 44 kDa. This 44-kDa fragment has been purified to homogeneity and characterized as a clathrin-independent ATPase. The 44-kDa ATPase domain has been localized within the intact enzyme by the use of amino-terminal specific antibodies. This localization relates to the conserved nature of the 70-kDa heat shock protein family, of which bovine brain uncoating ATPase is a constitutively expressed member.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / isolation & purification
  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins
  • Brain / enzymology*
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Cattle
  • Chymotrypsin / metabolism
  • Clathrin / isolation & purification
  • Clathrin / metabolism
  • HSC70 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins*
  • Rats

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Clathrin
  • HSC70 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • Hspa8 protein, rat
  • Chymotrypsin
  • Adenosine Triphosphatases