Article

Title:Identification of a Region of the Polypeptide Chain of Na,K-ATPase alpha-Subunit Interacting with 67-kDa Melittin-Like Protein.
Authors:Kamanina YV; Klimanova EA; Dergousova EA; Petrushanko IY; Lopina OD
Publication:Biochemistry (Mosc). 2016 Mar;81(3):249-54. doi: 10.1134/S000629791603007X.
PubmedID27262194
Abstract
It was shown earlier that a 67-kDa protein purified from mouse kidney using polyclonal antibodies against melittin (a peptide from bee venom) interacted with Na,K-ATPase from rabbit kidney. In this study, a 43-kDa proteolytic fragment of Na,K-ATPase alpha-subunit interacting with the 67-kDa melittin-like protein was found. The alpha-subunit was hydrolyzed by trypsin in the presence of 0.5 mM ouabain (E2-conformation of Na,K-ATPase). A proteolytic fragment interacting with the 67-kDa melittin-like protein that was identified by mass-spectrometry is a region of the cytoplasmic domain of Na,K-ATPase alpha-subunit located between amino acid residues 591 and 775. The fragment includes a conservative DPPRA motif that occurs in many P-type ATPases. It was shown earlier that this motif of H,K-ATPase from gastric mucosa binds to melittin. We suggest that namely this motif of P-type ATPases is able to interact with proteins containing melittin-like modules.