Carbonic Anhydrase Subunits Form a Matrix-exposed Domain Attached to the Membrane Arm of Mitochondrial Complex I in Plants

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

Externe Organisationen

  • Reichsuniversität Groningen
  • Helmholtz-Zentrum für Infektionsforschung GmbH (HZI)
  • Universidad Nacional de Mar del Plata
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)6482-6488
Seitenumfang7
FachzeitschriftJournal of Biological Chemistry
Jahrgang281
Ausgabenummer10
PublikationsstatusVeröffentlicht - 4 Jan. 2006

Abstract

Complex I of Arabidopsis includes five structurally related subunits representing γ-type carbonic anhydrases termed CA1, CA2, CA3, CAL1, and CAL2. The position of these subunits within complex I was investigated. Direct analysis of isolated subcomplexes of complex I by liquid chromatography linked to tandem mass spectrometry allowed the assignment of the CA subunits to the membrane arm of complex I. Carbonate extraction experiments revealed that CA2 is an integral membrane protein that is protected upon protease treatment of isolated mitoplasts, indicating a location on the matrix-exposed side of the complex. A structural characterization by single particle electron microscopy of complex I from the green alga Polytomella and a previous analysis from Arabidopsis indicate a plant-specific spherical extra-domain of about 60 Å in diameter, which is attached to the central part of the membrane arm of complex I on its matrix face. This spherical domain is proposed to contain a heterotrimer of three CA subunits, which are anchored with their C termini to the hydrophobic arm of complex I. Functional implications of the complex I-integrated CA subunits are discussed.

ASJC Scopus Sachgebiete

Zitieren

Carbonic Anhydrase Subunits Form a Matrix-exposed Domain Attached to the Membrane Arm of Mitochondrial Complex I in Plants. / Sunderhaus, Stephanie; Dudkina, Natalya V.; Jänsch, Lothar et al.
in: Journal of Biological Chemistry, Jahrgang 281, Nr. 10, 04.01.2006, S. 6482-6488.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Sunderhaus S, Dudkina NV, Jänsch L, Klodmann J, Heinemeyer J, Perales M et al. Carbonic Anhydrase Subunits Form a Matrix-exposed Domain Attached to the Membrane Arm of Mitochondrial Complex I in Plants. Journal of Biological Chemistry. 2006 Jan 4;281(10):6482-6488. doi: 10.1074/jbc.M511542200, 10.15488/11693
Sunderhaus, Stephanie ; Dudkina, Natalya V. ; Jänsch, Lothar et al. / Carbonic Anhydrase Subunits Form a Matrix-exposed Domain Attached to the Membrane Arm of Mitochondrial Complex I in Plants. in: Journal of Biological Chemistry. 2006 ; Jahrgang 281, Nr. 10. S. 6482-6488.
Download
@article{1aecde128a294051a6da37414dcb159d,
title = "Carbonic Anhydrase Subunits Form a Matrix-exposed Domain Attached to the Membrane Arm of Mitochondrial Complex I in Plants",
abstract = "Complex I of Arabidopsis includes five structurally related subunits representing γ-type carbonic anhydrases termed CA1, CA2, CA3, CAL1, and CAL2. The position of these subunits within complex I was investigated. Direct analysis of isolated subcomplexes of complex I by liquid chromatography linked to tandem mass spectrometry allowed the assignment of the CA subunits to the membrane arm of complex I. Carbonate extraction experiments revealed that CA2 is an integral membrane protein that is protected upon protease treatment of isolated mitoplasts, indicating a location on the matrix-exposed side of the complex. A structural characterization by single particle electron microscopy of complex I from the green alga Polytomella and a previous analysis from Arabidopsis indicate a plant-specific spherical extra-domain of about 60 {\AA} in diameter, which is attached to the central part of the membrane arm of complex I on its matrix face. This spherical domain is proposed to contain a heterotrimer of three CA subunits, which are anchored with their C termini to the hydrophobic arm of complex I. Functional implications of the complex I-integrated CA subunits are discussed.",
author = "Stephanie Sunderhaus and Dudkina, {Natalya V.} and Lothar J{\"a}nsch and Jennifer Klodmann and Jesco Heinemeyer and Mariano Perales and Eduardo Zabaleta and Boekema, {Egbert J.} and Braun, {Hans Peter}",
year = "2006",
month = jan,
day = "4",
doi = "10.1074/jbc.M511542200",
language = "English",
volume = "281",
pages = "6482--6488",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "10",

}

Download

TY - JOUR

T1 - Carbonic Anhydrase Subunits Form a Matrix-exposed Domain Attached to the Membrane Arm of Mitochondrial Complex I in Plants

AU - Sunderhaus, Stephanie

AU - Dudkina, Natalya V.

AU - Jänsch, Lothar

AU - Klodmann, Jennifer

AU - Heinemeyer, Jesco

AU - Perales, Mariano

AU - Zabaleta, Eduardo

AU - Boekema, Egbert J.

AU - Braun, Hans Peter

PY - 2006/1/4

Y1 - 2006/1/4

N2 - Complex I of Arabidopsis includes five structurally related subunits representing γ-type carbonic anhydrases termed CA1, CA2, CA3, CAL1, and CAL2. The position of these subunits within complex I was investigated. Direct analysis of isolated subcomplexes of complex I by liquid chromatography linked to tandem mass spectrometry allowed the assignment of the CA subunits to the membrane arm of complex I. Carbonate extraction experiments revealed that CA2 is an integral membrane protein that is protected upon protease treatment of isolated mitoplasts, indicating a location on the matrix-exposed side of the complex. A structural characterization by single particle electron microscopy of complex I from the green alga Polytomella and a previous analysis from Arabidopsis indicate a plant-specific spherical extra-domain of about 60 Å in diameter, which is attached to the central part of the membrane arm of complex I on its matrix face. This spherical domain is proposed to contain a heterotrimer of three CA subunits, which are anchored with their C termini to the hydrophobic arm of complex I. Functional implications of the complex I-integrated CA subunits are discussed.

AB - Complex I of Arabidopsis includes five structurally related subunits representing γ-type carbonic anhydrases termed CA1, CA2, CA3, CAL1, and CAL2. The position of these subunits within complex I was investigated. Direct analysis of isolated subcomplexes of complex I by liquid chromatography linked to tandem mass spectrometry allowed the assignment of the CA subunits to the membrane arm of complex I. Carbonate extraction experiments revealed that CA2 is an integral membrane protein that is protected upon protease treatment of isolated mitoplasts, indicating a location on the matrix-exposed side of the complex. A structural characterization by single particle electron microscopy of complex I from the green alga Polytomella and a previous analysis from Arabidopsis indicate a plant-specific spherical extra-domain of about 60 Å in diameter, which is attached to the central part of the membrane arm of complex I on its matrix face. This spherical domain is proposed to contain a heterotrimer of three CA subunits, which are anchored with their C termini to the hydrophobic arm of complex I. Functional implications of the complex I-integrated CA subunits are discussed.

UR - http://www.scopus.com/inward/record.url?scp=33646365010&partnerID=8YFLogxK

U2 - 10.1074/jbc.M511542200

DO - 10.1074/jbc.M511542200

M3 - Article

C2 - 16407270

AN - SCOPUS:33646365010

VL - 281

SP - 6482

EP - 6488

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 10

ER -

Von denselben Autoren