Characterization of Tic110, a channel-forming protein at the inner envelope membrane of chloroplasts, unveils a response to Ca2+ and a stromal regulatory disulfide bridge

Mónica Balsera, Tom A. Goetze, E. Kovács, Peter Schürmann, Richard Wagner, Bob B. Buchanan, Jürgen Soll, Bettina Bölter

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

Tic110 has been proposed to be a channel-forming protein at the inner envelope of chloroplasts whose function is essential for the import of proteins synthesized in the cytosol. Sequence features and topology determination experiments presently summarized suggest that Tic110 consists of six transmembrane helices. Its topology has been mapped by limited proteolysis experiments in combination with mass spectrometric determinations and cysteine modification analysis. Two hydrophobic transmembrane helices located in the N terminus serve as a signal for the localization of the protein to the membrane as shown previously. The other amphipathic transmembrane helices are located in the region composed of residues 92-959 in the pea sequence. This results in two regions in the intermembrane space localized to form supercomplexes with the TOC machinery and to receive the transit peptide of preproteins. A large region also resides in the stroma for interaction with proteins such as molecular chaperones. In addition to characterizing the topology of Tic110, we show that Ca2+ has a dramatic effect on channel activity in vitro and that the protein has a redox-active disulfide with the potential to interact with stromal thioredoxin.

Original languageEnglish
Pages (from-to)2603-2616
Number of pages14
JournalJournal of Biological Chemistry
Volume284
Issue number5
DOIs
Publication statusPublished - Jan 30 2009

Fingerprint

Chloroplasts
Disulfides
Membranes
Topology
Proteins
Thioredoxins
Molecular Chaperones
Proteolysis
Peas
Cytosol
Oxidation-Reduction
Cysteine
Membrane Proteins
Machinery
Peptides
Experiments

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Characterization of Tic110, a channel-forming protein at the inner envelope membrane of chloroplasts, unveils a response to Ca2+ and a stromal regulatory disulfide bridge. / Balsera, Mónica; Goetze, Tom A.; Kovács, E.; Schürmann, Peter; Wagner, Richard; Buchanan, Bob B.; Soll, Jürgen; Bölter, Bettina.

In: Journal of Biological Chemistry, Vol. 284, No. 5, 30.01.2009, p. 2603-2616.

Research output: Contribution to journalArticle

Balsera, Mónica ; Goetze, Tom A. ; Kovács, E. ; Schürmann, Peter ; Wagner, Richard ; Buchanan, Bob B. ; Soll, Jürgen ; Bölter, Bettina. / Characterization of Tic110, a channel-forming protein at the inner envelope membrane of chloroplasts, unveils a response to Ca2+ and a stromal regulatory disulfide bridge. In: Journal of Biological Chemistry. 2009 ; Vol. 284, No. 5. pp. 2603-2616.
@article{2055ca8f31684a909c11ae9866e1850f,
title = "Characterization of Tic110, a channel-forming protein at the inner envelope membrane of chloroplasts, unveils a response to Ca2+ and a stromal regulatory disulfide bridge",
abstract = "Tic110 has been proposed to be a channel-forming protein at the inner envelope of chloroplasts whose function is essential for the import of proteins synthesized in the cytosol. Sequence features and topology determination experiments presently summarized suggest that Tic110 consists of six transmembrane helices. Its topology has been mapped by limited proteolysis experiments in combination with mass spectrometric determinations and cysteine modification analysis. Two hydrophobic transmembrane helices located in the N terminus serve as a signal for the localization of the protein to the membrane as shown previously. The other amphipathic transmembrane helices are located in the region composed of residues 92-959 in the pea sequence. This results in two regions in the intermembrane space localized to form supercomplexes with the TOC machinery and to receive the transit peptide of preproteins. A large region also resides in the stroma for interaction with proteins such as molecular chaperones. In addition to characterizing the topology of Tic110, we show that Ca2+ has a dramatic effect on channel activity in vitro and that the protein has a redox-active disulfide with the potential to interact with stromal thioredoxin.",
author = "M{\'o}nica Balsera and Goetze, {Tom A.} and E. Kov{\'a}cs and Peter Sch{\"u}rmann and Richard Wagner and Buchanan, {Bob B.} and J{\"u}rgen Soll and Bettina B{\"o}lter",
year = "2009",
month = "1",
day = "30",
doi = "10.1074/jbc.M807134200",
language = "English",
volume = "284",
pages = "2603--2616",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "5",

}

TY - JOUR

T1 - Characterization of Tic110, a channel-forming protein at the inner envelope membrane of chloroplasts, unveils a response to Ca2+ and a stromal regulatory disulfide bridge

AU - Balsera, Mónica

AU - Goetze, Tom A.

AU - Kovács, E.

AU - Schürmann, Peter

AU - Wagner, Richard

AU - Buchanan, Bob B.

AU - Soll, Jürgen

AU - Bölter, Bettina

PY - 2009/1/30

Y1 - 2009/1/30

N2 - Tic110 has been proposed to be a channel-forming protein at the inner envelope of chloroplasts whose function is essential for the import of proteins synthesized in the cytosol. Sequence features and topology determination experiments presently summarized suggest that Tic110 consists of six transmembrane helices. Its topology has been mapped by limited proteolysis experiments in combination with mass spectrometric determinations and cysteine modification analysis. Two hydrophobic transmembrane helices located in the N terminus serve as a signal for the localization of the protein to the membrane as shown previously. The other amphipathic transmembrane helices are located in the region composed of residues 92-959 in the pea sequence. This results in two regions in the intermembrane space localized to form supercomplexes with the TOC machinery and to receive the transit peptide of preproteins. A large region also resides in the stroma for interaction with proteins such as molecular chaperones. In addition to characterizing the topology of Tic110, we show that Ca2+ has a dramatic effect on channel activity in vitro and that the protein has a redox-active disulfide with the potential to interact with stromal thioredoxin.

AB - Tic110 has been proposed to be a channel-forming protein at the inner envelope of chloroplasts whose function is essential for the import of proteins synthesized in the cytosol. Sequence features and topology determination experiments presently summarized suggest that Tic110 consists of six transmembrane helices. Its topology has been mapped by limited proteolysis experiments in combination with mass spectrometric determinations and cysteine modification analysis. Two hydrophobic transmembrane helices located in the N terminus serve as a signal for the localization of the protein to the membrane as shown previously. The other amphipathic transmembrane helices are located in the region composed of residues 92-959 in the pea sequence. This results in two regions in the intermembrane space localized to form supercomplexes with the TOC machinery and to receive the transit peptide of preproteins. A large region also resides in the stroma for interaction with proteins such as molecular chaperones. In addition to characterizing the topology of Tic110, we show that Ca2+ has a dramatic effect on channel activity in vitro and that the protein has a redox-active disulfide with the potential to interact with stromal thioredoxin.

UR - http://www.scopus.com/inward/record.url?scp=59149100724&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=59149100724&partnerID=8YFLogxK

U2 - 10.1074/jbc.M807134200

DO - 10.1074/jbc.M807134200

M3 - Article

C2 - 18986981

AN - SCOPUS:59149100724

VL - 284

SP - 2603

EP - 2616

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 5

ER -