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Association of the eukaryotic V1VO ATPase subunits a with d and d with A |
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| Authors: | Youg R Thaker Yin H Yau |
| Institution: | School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Republic of Singapore |
| 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 200 nM 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 summaryMINT-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) |
| Keywords: | DTT dithiothreitol FCS fluorescence correlation spectroscopy IPTG d-thio-galactoside" target="_blank">isopropyl-β-d-thio-galactoside NBD-Cl 7-chloro-4-nitrobenzo-2-oxa-1 3-diazole NHR non-homologous region NTA nitrilotriacetic acid PAGE polyacrylamide gel electrophoresis PCR polymerase chain reaction SAXS small angle X-ray scattering SDS sodium dodecyl sulfate SPR surface plasmon resonance TMR tetramethylrhodamin Tris Tris-(hydroxymethyl) aminomethane |
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