Identification of a region of the polypeptide chain of Na,K-ATPase α-subunit interacting with 67-kDa melittin-like protein
- Authors: Kamanina Y.V.1,2, Klimanova E.A.1,2, Dergousova E.A.1,2, Petrushanko I.Y.2, Lopina O.D.1
- 
							Affiliations: 
							- Department of Biochemistry, School of Biology
- Engelhardt Institute of Molecular Biology
 
- Issue: Vol 81, No 3 (2016)
- Pages: 249-254
- Section: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150802
- DOI: https://doi.org/10.1134/S000629791603007X
- ID: 150802
Cite item
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 α-subunit interacting with the 67-kDa melittin-like protein was found. The α-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 α-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.
About the authors
Yu. V. Kamanina
Department of Biochemistry, School of Biology; Engelhardt Institute of Molecular Biology
														Email: od_lopina@mail.ru
				                					                																			                												                	Russian Federation, 							Moscow, 119991; Moscow, 119991						
E. A. Klimanova
Department of Biochemistry, School of Biology; Engelhardt Institute of Molecular Biology
														Email: od_lopina@mail.ru
				                					                																			                												                	Russian Federation, 							Moscow, 119991; Moscow, 119991						
E. A. Dergousova
Department of Biochemistry, School of Biology; Engelhardt Institute of Molecular Biology
														Email: od_lopina@mail.ru
				                					                																			                												                	Russian Federation, 							Moscow, 119991; Moscow, 119991						
I. Yu. Petrushanko
Engelhardt Institute of Molecular Biology
														Email: od_lopina@mail.ru
				                					                																			                												                	Russian Federation, 							Moscow, 119991						
O. D. Lopina
Department of Biochemistry, School of Biology
							Author for correspondence.
							Email: od_lopina@mail.ru
				                					                																			                												                	Russian Federation, 							Moscow, 119991						
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