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

Youg R. Thaker; Cornelia Hunke; Yin H. Yau; Susana Geifman Shochat; Ying Li; Gerhard Grüber

doi:10.1016/j.febslet.2009.03.013

Association of the eukaryotic V₁V_O ATPase subunits a with d and d with A

Youg R. Thaker, Cornelia Hunke, Yin H. Yau, Susana Geifman Shochat, Ying Li, Gerhard Grüber^*

^*Corresponding author for this work

Nanyang Technological University

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

Owing to the complex nature of V₁V_O ATPases, identification of neighboring subunits is essential for mechanistic understanding of this enzyme. Here, we describe the links between the V₁ headpiece and the V_O-domain of the yeast V₁V_O ATPase via subunit A and d as well as the V_O 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 V_O. 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).

Original language	English
Pages (from-to)	1090-1095
Number of pages	6
Journal	FEBS Letters
Volume	583
Issue number	7
DOIs	https://doi.org/10.1016/j.febslet.2009.03.013
Publication status	Published - Apr 2 2009
Externally published	Yes

ASJC Scopus Subject Areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

NBD-Cl
Subunit A
Subunit a
Subunit d
Surface plasmon resonance
VV ATPase
Vacuolar-type ATPase

Access to Document

10.1016/j.febslet.2009.03.013

Cite this

@article{ab8d989149934341aaf14034986cd5ab,

title = "Association of the eukaryotic V1VO ATPase subunits a with d and d with A",

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 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).",

keywords = "NBD-Cl, Subunit A, Subunit a, Subunit d, Surface plasmon resonance, VV ATPase, Vacuolar-type ATPase",

author = "Thaker, {Youg R.} and Cornelia Hunke and Yau, {Yin H.} and Shochat, {Susana Geifman} and Ying Li and Gerhard Gr{\"u}ber",

year = "2009",

month = apr,

day = "2",

doi = "10.1016/j.febslet.2009.03.013",

language = "English",

volume = "583",

pages = "1090--1095",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "7",

}

TY - JOUR

T1 - Association of the eukaryotic V1VO ATPase subunits a with d and d with A

AU - Thaker, Youg R.

AU - Hunke, Cornelia

AU - Yau, Yin H.

AU - Shochat, Susana Geifman

AU - Li, Ying

AU - Grüber, Gerhard

PY - 2009/4/2

Y1 - 2009/4/2

N2 - 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 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).

AB - 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 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).

KW - NBD-Cl

KW - Subunit A

KW - Subunit a

KW - Subunit d

KW - Surface plasmon resonance

KW - VV ATPase

KW - Vacuolar-type ATPase

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