Purification characterization of the inhibitory subunit (δ) of the ATP-synthase from Micrococcus luteus

Gerhard Grüber; Siegfried Engelbrecht; Wolfgang Junge; Klaus Dose; Thomas Nawroth

doi:10.1016/0014-5793(94)01271-7

Purification characterization of the inhibitory subunit (δ) of the ATP-synthase from Micrococcus luteus

Gerhard Grüber^*, Siegfried Engelbrecht, Wolfgang Junge, Klaus Dose, Thomas Nawroth

^*Corresponding author for this work

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

3 Citations (Scopus)

Abstract

Subunit δ was isolated from the ATP-synthase from Micrococcus luteus strain (ATCC 4698). δ, in the case of M. luteus F₀F₁-ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP-synthase. After treatment with 1.5 M LiCl the ATP-synthase dissociated, and subsequently subunit δ (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP-synthase lacking δ by addition of δ showed noncompetitive kinetics with a K_i of ∼ 5.9nM. Subunit ε from chloroplast F₁, which corresponds functionally to the M. luteus F₀F₁-δ, and chloroplast δ were tested for ATPase inhibitory activity by addition to the partially δ-depleted ATP-synthase from M. luteus. CF₁-ε inhibited M. luteus ATP-synthase up to 80%, whereas CF₁-δ did not show any influence.

Original language	English
Pages (from-to)	226-228
Number of pages	3
Journal	FEBS Letters
Volume	356
Issue number	2-3
DOIs	https://doi.org/10.1016/0014-5793(94)01271-7
Publication status	Published - Dec 19 1994
Externally published	Yes

ASJC Scopus Subject Areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

ATP-synthase
CF
Inhibitor protein
Micrococcus luteus
Reconstitution
δ subunit
ε subunit

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10.1016/0014-5793(94)01271-7

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title = "Purification characterization of the inhibitory subunit (δ) of the ATP-synthase from Micrococcus luteus",

abstract = "Subunit δ was isolated from the ATP-synthase from Micrococcus luteus strain (ATCC 4698). δ, in the case of M. luteus F0F1-ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP-synthase. After treatment with 1.5 M LiCl the ATP-synthase dissociated, and subsequently subunit δ (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP-synthase lacking δ by addition of δ showed noncompetitive kinetics with a Ki of ∼ 5.9nM. Subunit ε from chloroplast F1, which corresponds functionally to the M. luteus F0F1-δ, and chloroplast δ were tested for ATPase inhibitory activity by addition to the partially δ-depleted ATP-synthase from M. luteus. CF1-ε inhibited M. luteus ATP-synthase up to 80\%, whereas CF1-δ did not show any influence.",

keywords = "ATP-synthase, CF, Inhibitor protein, Micrococcus luteus, Reconstitution, δ subunit, ε subunit",

author = "Gerhard Gr{\"u}ber and Siegfried Engelbrecht and Wolfgang Junge and Klaus Dose and Thomas Nawroth",

year = "1994",

month = dec,

day = "19",

doi = "10.1016/0014-5793(94)01271-7",

language = "English",

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journal = "FEBS Letters",

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T1 - Purification characterization of the inhibitory subunit (δ) of the ATP-synthase from Micrococcus luteus

AU - Grüber, Gerhard

AU - Engelbrecht, Siegfried

AU - Junge, Wolfgang

AU - Dose, Klaus

AU - Nawroth, Thomas

PY - 1994/12/19

Y1 - 1994/12/19

N2 - Subunit δ was isolated from the ATP-synthase from Micrococcus luteus strain (ATCC 4698). δ, in the case of M. luteus F0F1-ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP-synthase. After treatment with 1.5 M LiCl the ATP-synthase dissociated, and subsequently subunit δ (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP-synthase lacking δ by addition of δ showed noncompetitive kinetics with a Ki of ∼ 5.9nM. Subunit ε from chloroplast F1, which corresponds functionally to the M. luteus F0F1-δ, and chloroplast δ were tested for ATPase inhibitory activity by addition to the partially δ-depleted ATP-synthase from M. luteus. CF1-ε inhibited M. luteus ATP-synthase up to 80%, whereas CF1-δ did not show any influence.

AB - Subunit δ was isolated from the ATP-synthase from Micrococcus luteus strain (ATCC 4698). δ, in the case of M. luteus F0F1-ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP-synthase. After treatment with 1.5 M LiCl the ATP-synthase dissociated, and subsequently subunit δ (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP-synthase lacking δ by addition of δ showed noncompetitive kinetics with a Ki of ∼ 5.9nM. Subunit ε from chloroplast F1, which corresponds functionally to the M. luteus F0F1-δ, and chloroplast δ were tested for ATPase inhibitory activity by addition to the partially δ-depleted ATP-synthase from M. luteus. CF1-ε inhibited M. luteus ATP-synthase up to 80%, whereas CF1-δ did not show any influence.

KW - ATP-synthase

KW - CF

KW - Inhibitor protein

KW - Micrococcus luteus

KW - Reconstitution

KW - δ subunit

KW - ε subunit

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ER -

Purification characterization of the inhibitory subunit (δ) of the ATP-synthase from Micrococcus luteus

Abstract

ASJC Scopus Subject Areas

Keywords

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