ATP synthase: Subunit-subunit interactions in the stator stalk

Joachim Weber

doi:10.1016/j.bbabio.2006.04.007

ATP synthase: Subunit-subunit interactions in the stator stalk

Joachim Weber

Chemistry and Biochemistry

Research output: Contribution to journal › Review article › peer-review

54 Scopus citations

Abstract

In ATP synthase, proton translocation through the F_o subcomplex and ATP synthesis/hydrolysis in the F₁ subcomplex are coupled by subunit rotation. The static, non-rotating portions of F₁ and F_o are attached to each other via the peripheral "stator stalk", which has to withstand elastic strain during subunit rotation. In Escherichia coli, the stator stalk consists of subunits b₂δ; in other organisms, it has three or four different subunits. Recent advances in this area include affinity measurements between individual components of the stator stalk as well as a detailed analysis of the interaction between subunit δ (or its mitochondrial counterpart, the oligomycin-sensitivity conferring protein, OSCP) and F₁. The current status of our knowledge of the structure of the stator stalk and of the interactions between its subunits will be discussed in this review.

Original language	English
Pages (from-to)	1162-1170
Number of pages	9
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	1757
Issue number	9-10
DOIs	https://doi.org/10.1016/j.bbabio.2006.04.007
State	Published - Sep 2006

Keywords

ATP synthase
F-ATPase
Peripheral stalk
Stator
Stator stalk

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10.1016/j.bbabio.2006.04.007

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title = "ATP synthase: Subunit-subunit interactions in the stator stalk",

abstract = "In ATP synthase, proton translocation through the Fo subcomplex and ATP synthesis/hydrolysis in the F1 subcomplex are coupled by subunit rotation. The static, non-rotating portions of F1 and Fo are attached to each other via the peripheral {"}stator stalk{"}, which has to withstand elastic strain during subunit rotation. In Escherichia coli, the stator stalk consists of subunits b2δ; in other organisms, it has three or four different subunits. Recent advances in this area include affinity measurements between individual components of the stator stalk as well as a detailed analysis of the interaction between subunit δ (or its mitochondrial counterpart, the oligomycin-sensitivity conferring protein, OSCP) and F1. The current status of our knowledge of the structure of the stator stalk and of the interactions between its subunits will be discussed in this review.",

keywords = "ATP synthase, F-ATPase, Peripheral stalk, Stator, Stator stalk",

author = "Joachim Weber",

note = "Funding Information: Work in the author's lab is supported by NIH grant GM071462. ",

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T2 - Subunit-subunit interactions in the stator stalk

AU - Weber, Joachim

N1 - Funding Information: Work in the author's lab is supported by NIH grant GM071462.

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N2 - In ATP synthase, proton translocation through the Fo subcomplex and ATP synthesis/hydrolysis in the F1 subcomplex are coupled by subunit rotation. The static, non-rotating portions of F1 and Fo are attached to each other via the peripheral "stator stalk", which has to withstand elastic strain during subunit rotation. In Escherichia coli, the stator stalk consists of subunits b2δ; in other organisms, it has three or four different subunits. Recent advances in this area include affinity measurements between individual components of the stator stalk as well as a detailed analysis of the interaction between subunit δ (or its mitochondrial counterpart, the oligomycin-sensitivity conferring protein, OSCP) and F1. The current status of our knowledge of the structure of the stator stalk and of the interactions between its subunits will be discussed in this review.

AB - In ATP synthase, proton translocation through the Fo subcomplex and ATP synthesis/hydrolysis in the F1 subcomplex are coupled by subunit rotation. The static, non-rotating portions of F1 and Fo are attached to each other via the peripheral "stator stalk", which has to withstand elastic strain during subunit rotation. In Escherichia coli, the stator stalk consists of subunits b2δ; in other organisms, it has three or four different subunits. Recent advances in this area include affinity measurements between individual components of the stator stalk as well as a detailed analysis of the interaction between subunit δ (or its mitochondrial counterpart, the oligomycin-sensitivity conferring protein, OSCP) and F1. The current status of our knowledge of the structure of the stator stalk and of the interactions between its subunits will be discussed in this review.

KW - ATP synthase

KW - F-ATPase

KW - Peripheral stalk

KW - Stator

KW - Stator stalk

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DO - 10.1016/j.bbabio.2006.04.007

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SN - 0005-2728

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JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

IS - 9-10

ER -

ATP synthase: Subunit-subunit interactions in the stator stalk

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