Complex formation of 70-kDa heat shock protein with acidic glycolipids and phospholipids.
A new property of a heat-inducible heat shock protein (Hsp) 70.1 that it forms a complex with acidic lipids was first demonstrated. Based on the behaviors of the complexes on the native PAGE, the acidic lipid/Hsp70.1 complexes are categorized into two groups. The first group is the sulfatide-induced large-sized complex, which stays on the gel top on the native PAGE. Only the N-terminal ATPase domain is responsible for the complex formation. The second group is the ganglioside-induced complex, which is diffused in the resolution gel on the native PAGE. Both the N-terminal ATPase and the C-terminal peptide-binding domains are involved in the complex formation. No complex is formed by neutral glyco- and phospholipids. The complex formation with the acidic glyco- and phospholipids implicates the various functions of Hsp70 on the membrane surfaces.
Harada
Yoichiro
Y
Laboratory of Animal Cell Fuction, Bioscience and Biotechnology Center, Nagoya University, Japan.
Sato
Chihiro
C
Kitajima
Ken
K
D000818:Animals; D006017:Glycolipids / Q000737:chemistry*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D051379:Mice; D010743:Phospholipids / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D013433:Sulfoglycosphingolipids / Q000737:chemistry
D006017:Glycolipids; D018840:HSP70 Heat-Shock Proteins; D010743:Phospholipids; D011994:Recombinant Proteins; D013433:Sulfoglycosphingolipids; C081884:heat-shock protein 70.1