The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity

Marco Zancani; Valentino Casolo; Carlo Peresson; Giorgio Federici; Andrea Urbani; Francesco Macrì; Angelo Vianello

doi:10.1016/S1567-7249(03)00105-3

The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity

Marco Zancani, Valentino Casolo, Carlo Peresson, Giorgio Federici, Andrea Urbani, Francesco Macrì, Angelo Vianello

Fondazione Santa Lucia

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

Abstract

A soluble protein with a molecular mass of 55 kDa has been purified from etiolated pea stem mitochondria. The protein exhibits a Mg²⁺-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F^-, Ca²⁺, aminomethylenediphosphate and imidodiphosphate. The protein does not cross-react with polyclonal antibodies raised against vacuolar, mitochondrial or soluble PPiases, respectively. Conversely, it cross-reacts with an antibody for the α/β-subunit of the ATP synthase from beef heart mitochondria. The purified protein has been analyzed by MALDI-TOF mass spectrometry and the results, covering the 30% of assigned sequence, indicate that it corresponds to the β-subunit of the ATP synthase of pea mitochondria. It is suggested that this enzymatic protein may perform a dual function as soluble PPiase or as subunit of the more complex ATP synthase.

Original language	English
Pages (from-to)	111-118
Number of pages	8
Journal	Mitochondrion
Volume	3
Issue number	2
DOIs	https://doi.org/10.1016/S1567-7249(03)00105-3
Publication status	Published - Oct 2003

Keywords

β-Subunit
ATP synthase
MALDI-TOF
Mitochondria
Pisum sativum
PPiase

ASJC Scopus subject areas

Biophysics

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10.1016/S1567-7249(03)00105-3

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title = "The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity",

abstract = "A soluble protein with a molecular mass of 55 kDa has been purified from etiolated pea stem mitochondria. The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. The protein does not cross-react with polyclonal antibodies raised against vacuolar, mitochondrial or soluble PPiases, respectively. Conversely, it cross-reacts with an antibody for the α/β-subunit of the ATP synthase from beef heart mitochondria. The purified protein has been analyzed by MALDI-TOF mass spectrometry and the results, covering the 30% of assigned sequence, indicate that it corresponds to the β-subunit of the ATP synthase of pea mitochondria. It is suggested that this enzymatic protein may perform a dual function as soluble PPiase or as subunit of the more complex ATP synthase.",

keywords = "β-Subunit, ATP synthase, MALDI-TOF, Mitochondria, Pisum sativum, PPiase",

author = "Marco Zancani and Valentino Casolo and Carlo Peresson and Giorgio Federici and Andrea Urbani and Francesco Macr{\`i} and Angelo Vianello",

year = "2003",

month = oct,

doi = "10.1016/S1567-7249(03)00105-3",

language = "English",

volume = "3",

pages = "111--118",

journal = "Mitochondrion",

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T1 - The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity

AU - Zancani, Marco

AU - Casolo, Valentino

AU - Peresson, Carlo

AU - Federici, Giorgio

AU - Urbani, Andrea

AU - Macrì, Francesco

AU - Vianello, Angelo

PY - 2003/10

Y1 - 2003/10

N2 - A soluble protein with a molecular mass of 55 kDa has been purified from etiolated pea stem mitochondria. The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. The protein does not cross-react with polyclonal antibodies raised against vacuolar, mitochondrial or soluble PPiases, respectively. Conversely, it cross-reacts with an antibody for the α/β-subunit of the ATP synthase from beef heart mitochondria. The purified protein has been analyzed by MALDI-TOF mass spectrometry and the results, covering the 30% of assigned sequence, indicate that it corresponds to the β-subunit of the ATP synthase of pea mitochondria. It is suggested that this enzymatic protein may perform a dual function as soluble PPiase or as subunit of the more complex ATP synthase.

AB - A soluble protein with a molecular mass of 55 kDa has been purified from etiolated pea stem mitochondria. The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. The protein does not cross-react with polyclonal antibodies raised against vacuolar, mitochondrial or soluble PPiases, respectively. Conversely, it cross-reacts with an antibody for the α/β-subunit of the ATP synthase from beef heart mitochondria. The purified protein has been analyzed by MALDI-TOF mass spectrometry and the results, covering the 30% of assigned sequence, indicate that it corresponds to the β-subunit of the ATP synthase of pea mitochondria. It is suggested that this enzymatic protein may perform a dual function as soluble PPiase or as subunit of the more complex ATP synthase.

KW - β-Subunit

KW - ATP synthase

KW - MALDI-TOF

KW - Mitochondria

KW - Pisum sativum

KW - PPiase

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AN - SCOPUS:0141573157

SN - 1567-7249

VL - 3

SP - 111

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JO - Mitochondrion

JF - Mitochondrion

IS - 2

ER -

The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

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