Identification of novel subunits of the TOM complex from Arabidopsis thaliana

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OriginalspracheEnglisch
Seiten (von - bis)407-416
Seitenumfang10
FachzeitschriftPlant physiology and biochemistry
Jahrgang41
Ausgabenummer5
PublikationsstatusVeröffentlicht - 23 Mai 2003

Abstract

The preprotein translocase of the outer mitochondrial membrane (also called TOM complex) from A rabidopsis thaliana was characterized by Blue-native gel electrophoresis (BN-PAGE) and Electrospray Tandem Mass Spectrometry (ESI-MS/MS). BN-PAGE allows to prepare a very stable 390 kDa complex that includes six different protein types: the 34 kDa translocation pore TOM40, the 21/23 kDa preprotein receptor TOM20, the small TOM component TOM7 and three further subunits of 10, 6.3 and 6.0 kDa. Primary structures of all TOM subunits were elucidated. The 10 kDa subunit represents a truncated version of the TOM22 preprotein receptor and the two 6 kDa proteins represent subunits possibly homologous to fungal TOM6 and TOM5, although sequence conservation is at the borderline of significance. TOM40, TOM7 and one or both of the 6 kDa subunits form a subcomplex of about 100 kDa. The six TOM proteins from A rabidopsis are encoded by 12 genes, at least 11 of which are expressed. While the subunit composition of the TOM complex from fungi, animals and plants is remarkably conserved, the domain structure of individual TOM proteins differs, e.g. acidic domains in TOM22 and the 6 kDa TOM subunits from Arabidopsis are absent. The domain structure of the Arabidopsis TOM complex does not support the so-called 'acid chain hypothesis', which explains the translocation of proteins across the outer mitochondrial membrane of mitochondria by the binding of preproteins to acidic protein domains within the TOM complex. Functional implications are discussed.

ASJC Scopus Sachgebiete

  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Physiologie
  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Genetik
  • Agrar- und Biowissenschaften (insg.)
  • Pflanzenkunde

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Identification of novel subunits of the TOM complex from Arabidopsis thaliana. / Werhahn, Wolf; Jänsch, Lothar; Braun, Hans Peter.
in: Plant physiology and biochemistry, Jahrgang 41, Nr. 5, 23.05.2003, S. 407-416.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Werhahn W, Jänsch L, Braun HP. Identification of novel subunits of the TOM complex from Arabidopsis thaliana. Plant physiology and biochemistry. 2003 Mai 23;41(5):407-416. doi: 10.1016/S0981-9428(03)00047-0
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title = "Identification of novel subunits of the TOM complex from Arabidopsis thaliana",
abstract = "The preprotein translocase of the outer mitochondrial membrane (also called TOM complex) from A rabidopsis thaliana was characterized by Blue-native gel electrophoresis (BN-PAGE) and Electrospray Tandem Mass Spectrometry (ESI-MS/MS). BN-PAGE allows to prepare a very stable 390 kDa complex that includes six different protein types: the 34 kDa translocation pore TOM40, the 21/23 kDa preprotein receptor TOM20, the small TOM component TOM7 and three further subunits of 10, 6.3 and 6.0 kDa. Primary structures of all TOM subunits were elucidated. The 10 kDa subunit represents a truncated version of the TOM22 preprotein receptor and the two 6 kDa proteins represent subunits possibly homologous to fungal TOM6 and TOM5, although sequence conservation is at the borderline of significance. TOM40, TOM7 and one or both of the 6 kDa subunits form a subcomplex of about 100 kDa. The six TOM proteins from A rabidopsis are encoded by 12 genes, at least 11 of which are expressed. While the subunit composition of the TOM complex from fungi, animals and plants is remarkably conserved, the domain structure of individual TOM proteins differs, e.g. acidic domains in TOM22 and the 6 kDa TOM subunits from Arabidopsis are absent. The domain structure of the Arabidopsis TOM complex does not support the so-called 'acid chain hypothesis', which explains the translocation of proteins across the outer mitochondrial membrane of mitochondria by the binding of preproteins to acidic protein domains within the TOM complex. Functional implications are discussed.",
keywords = "Arabidopsis thaliana, Mitochondria, Protein import apparatus, TOM complex, TOM22",
author = "Wolf Werhahn and Lothar J{\"a}nsch and Braun, {Hans Peter}",
note = "Funding information: We thank Gabi K{\"u}hne, Dagmar Lewejohann and Ingrid Robotta for the cultivation of Arabidopsis cell lines and expert technical assistance. Our work was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.",
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TY - JOUR

T1 - Identification of novel subunits of the TOM complex from Arabidopsis thaliana

AU - Werhahn, Wolf

AU - Jänsch, Lothar

AU - Braun, Hans Peter

N1 - Funding information: We thank Gabi Kühne, Dagmar Lewejohann and Ingrid Robotta for the cultivation of Arabidopsis cell lines and expert technical assistance. Our work was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.

PY - 2003/5/23

Y1 - 2003/5/23

N2 - The preprotein translocase of the outer mitochondrial membrane (also called TOM complex) from A rabidopsis thaliana was characterized by Blue-native gel electrophoresis (BN-PAGE) and Electrospray Tandem Mass Spectrometry (ESI-MS/MS). BN-PAGE allows to prepare a very stable 390 kDa complex that includes six different protein types: the 34 kDa translocation pore TOM40, the 21/23 kDa preprotein receptor TOM20, the small TOM component TOM7 and three further subunits of 10, 6.3 and 6.0 kDa. Primary structures of all TOM subunits were elucidated. The 10 kDa subunit represents a truncated version of the TOM22 preprotein receptor and the two 6 kDa proteins represent subunits possibly homologous to fungal TOM6 and TOM5, although sequence conservation is at the borderline of significance. TOM40, TOM7 and one or both of the 6 kDa subunits form a subcomplex of about 100 kDa. The six TOM proteins from A rabidopsis are encoded by 12 genes, at least 11 of which are expressed. While the subunit composition of the TOM complex from fungi, animals and plants is remarkably conserved, the domain structure of individual TOM proteins differs, e.g. acidic domains in TOM22 and the 6 kDa TOM subunits from Arabidopsis are absent. The domain structure of the Arabidopsis TOM complex does not support the so-called 'acid chain hypothesis', which explains the translocation of proteins across the outer mitochondrial membrane of mitochondria by the binding of preproteins to acidic protein domains within the TOM complex. Functional implications are discussed.

AB - The preprotein translocase of the outer mitochondrial membrane (also called TOM complex) from A rabidopsis thaliana was characterized by Blue-native gel electrophoresis (BN-PAGE) and Electrospray Tandem Mass Spectrometry (ESI-MS/MS). BN-PAGE allows to prepare a very stable 390 kDa complex that includes six different protein types: the 34 kDa translocation pore TOM40, the 21/23 kDa preprotein receptor TOM20, the small TOM component TOM7 and three further subunits of 10, 6.3 and 6.0 kDa. Primary structures of all TOM subunits were elucidated. The 10 kDa subunit represents a truncated version of the TOM22 preprotein receptor and the two 6 kDa proteins represent subunits possibly homologous to fungal TOM6 and TOM5, although sequence conservation is at the borderline of significance. TOM40, TOM7 and one or both of the 6 kDa subunits form a subcomplex of about 100 kDa. The six TOM proteins from A rabidopsis are encoded by 12 genes, at least 11 of which are expressed. While the subunit composition of the TOM complex from fungi, animals and plants is remarkably conserved, the domain structure of individual TOM proteins differs, e.g. acidic domains in TOM22 and the 6 kDa TOM subunits from Arabidopsis are absent. The domain structure of the Arabidopsis TOM complex does not support the so-called 'acid chain hypothesis', which explains the translocation of proteins across the outer mitochondrial membrane of mitochondria by the binding of preproteins to acidic protein domains within the TOM complex. Functional implications are discussed.

KW - Arabidopsis thaliana

KW - Mitochondria

KW - Protein import apparatus

KW - TOM complex

KW - TOM22

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U2 - 10.1016/S0981-9428(03)00047-0

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VL - 41

SP - 407

EP - 416

JO - Plant physiology and biochemistry

JF - Plant physiology and biochemistry

SN - 0981-9428

IS - 5

ER -

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