Association of the eukaryotic V1VO ATPase subunits a with d and d with A

Autor:	Thaker, Youg R., Hunke, Cornelia, Yau, Yin H., Shochat, Susana Geifman, Li, Ying, Grüber, Gerhard
Předmět:	EUKARYOTIC cells ADENOSINE triphosphatase MOLECULAR association ENZYME kinetics YEAST SURFACE plasmon resonance FLUORESCENCE spectroscopy BINDING sites
Zdroj:	FEBS Letters; Apr2009, Vol. 583 Issue 7, p1090-1095, 6p
Abstrakt:	Abstract: Owing to the complex nature of V1VO ATPases, identification of neighboring subunits is essential for mechanistic understanding of this enzyme. Here, we describe the links between the V1 headpiece and the VO-domain of the yeast V1VO ATPase via subunit A and d as well as the VO subunits a and d using surface plasmon resonance and fluorescence correlation spectroscopy. Binding constants of about 60 and 200nM have been determined for the a–d and d–A assembly, respectively. The data are discussed in light of subunit a and d forming a peripheral stalk, connecting the catalytic A3B3 hexamer with VO. Structured summary: MINT-7012054: d (uniprotkb:P32366) binds (MI:0407) to A (uniprotkb:P17255) by fluorescence correlation spectroscopy (MI:0052) MINT-7012041: d (uniprotkb:P32366) binds (MI:0407) to A (uniprotkb:P17255) by surface plasmon resonance (MI:0107) MINT-7012028: d (uniprotkb:P32366) binds (MI:0407) to a (uniprotkb:P32563) by surface plasmon resonance (MI:0107) [Copyright &y& Elsevier]
Databáze:	Complementary Index
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