The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat

Hiroshi Suzuki; Yasuyuki Ito; Yuji Yamazaki; Katsuhiko Mineta; Masami Uji; Kazuhiro Abe; Kazutoshi Tani; Yoshinori Fujiyoshi; Sachiko Tsukita

doi:10.1038/ncomms2731

The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat

Hiroshi Suzuki, Yasuyuki Ito, Yuji Yamazaki, Katsuhiko Mineta, Masami Uji, Kazuhiro Abe, Kazutoshi Tani, Yoshinori Fujiyoshi^*, Sachiko Tsukita

^*Corresponding author for this work

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

17 Scopus citations

Abstract

Euglenoid flagellates have striped surface structures comprising pellicles, which allow the cell shape to vary from rigid to flexible during the characteristic movement of the flagellates. In Euglena gracilis, the pellicular strip membranes are covered with paracrystalline arrays of a major integral membrane protein, IP39, a putative four-membrane-spanning protein with the conserved sequence motif of the PMP-22/EMP/MP20/Claudin superfamily. Here we report the three-dimensional structure of Euglena IP39 determined by electron crystallography. Two-dimensional crystals of IP39 appear to form a striated pattern of antiparallel double-rows in which trimeric IP39 units are longitudinally polymerised, resulting in continuously extending zigzag-shaped lines. Structural analysis revealed an asymmetric molecular arrangement in the trimer, and suggested that at least four different interactions between neighbouring protomers are involved. A combination of such multiple interactions would be important for linear strand formation of membrane proteins in a lipid bilayer.

Original language	English (US)
Article number	1766
Journal	Nature Communications
Volume	4
DOIs	https://doi.org/10.1038/ncomms2731
State	Published - 2013
Externally published	Yes

Bibliographical note

Funding Information:
We appreciate Dr T. Suzaki (Kobe University) for kindly providing the Euglena gracilis strain and anti-IP39 antibodies. We also thank Mr K. Kobayashi (JEOL) for technical assistance with the electron microscopy. This work was supported in part by Grants-in-Aid for JSPS Fellows (23 5494) (to Y.I.), for Young Scientists (B) (to K.T.), for Scientific Research (S) (to Y.F.) and (A) (to S.T.), for Creative Scientific Research (to S.T.) from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and by Japan New Energy and Industrial Technology Development Organization (to Y.F.).

ASJC Scopus subject areas

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

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Cite this

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title = "The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat",

abstract = "Euglenoid flagellates have striped surface structures comprising pellicles, which allow the cell shape to vary from rigid to flexible during the characteristic movement of the flagellates. In Euglena gracilis, the pellicular strip membranes are covered with paracrystalline arrays of a major integral membrane protein, IP39, a putative four-membrane-spanning protein with the conserved sequence motif of the PMP-22/EMP/MP20/Claudin superfamily. Here we report the three-dimensional structure of Euglena IP39 determined by electron crystallography. Two-dimensional crystals of IP39 appear to form a striated pattern of antiparallel double-rows in which trimeric IP39 units are longitudinally polymerised, resulting in continuously extending zigzag-shaped lines. Structural analysis revealed an asymmetric molecular arrangement in the trimer, and suggested that at least four different interactions between neighbouring protomers are involved. A combination of such multiple interactions would be important for linear strand formation of membrane proteins in a lipid bilayer.",

author = "Hiroshi Suzuki and Yasuyuki Ito and Yuji Yamazaki and Katsuhiko Mineta and Masami Uji and Kazuhiro Abe and Kazutoshi Tani and Yoshinori Fujiyoshi and Sachiko Tsukita",

note = "Funding Information: We appreciate Dr T. Suzaki (Kobe University) for kindly providing the Euglena gracilis strain and anti-IP39 antibodies. We also thank Mr K. Kobayashi (JEOL) for technical assistance with the electron microscopy. This work was supported in part by Grants-in-Aid for JSPS Fellows (23 5494) (to Y.I.), for Young Scientists (B) (to K.T.), for Scientific Research (S) (to Y.F.) and (A) (to S.T.), for Creative Scientific Research (to S.T.) from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and by Japan New Energy and Industrial Technology Development Organization (to Y.F.).",

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AU - Suzuki, Hiroshi

AU - Ito, Yasuyuki

AU - Yamazaki, Yuji

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AU - Abe, Kazuhiro

AU - Tani, Kazutoshi

AU - Fujiyoshi, Yoshinori

AU - Tsukita, Sachiko

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PY - 2013

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N2 - Euglenoid flagellates have striped surface structures comprising pellicles, which allow the cell shape to vary from rigid to flexible during the characteristic movement of the flagellates. In Euglena gracilis, the pellicular strip membranes are covered with paracrystalline arrays of a major integral membrane protein, IP39, a putative four-membrane-spanning protein with the conserved sequence motif of the PMP-22/EMP/MP20/Claudin superfamily. Here we report the three-dimensional structure of Euglena IP39 determined by electron crystallography. Two-dimensional crystals of IP39 appear to form a striated pattern of antiparallel double-rows in which trimeric IP39 units are longitudinally polymerised, resulting in continuously extending zigzag-shaped lines. Structural analysis revealed an asymmetric molecular arrangement in the trimer, and suggested that at least four different interactions between neighbouring protomers are involved. A combination of such multiple interactions would be important for linear strand formation of membrane proteins in a lipid bilayer.

AB - Euglenoid flagellates have striped surface structures comprising pellicles, which allow the cell shape to vary from rigid to flexible during the characteristic movement of the flagellates. In Euglena gracilis, the pellicular strip membranes are covered with paracrystalline arrays of a major integral membrane protein, IP39, a putative four-membrane-spanning protein with the conserved sequence motif of the PMP-22/EMP/MP20/Claudin superfamily. Here we report the three-dimensional structure of Euglena IP39 determined by electron crystallography. Two-dimensional crystals of IP39 appear to form a striated pattern of antiparallel double-rows in which trimeric IP39 units are longitudinally polymerised, resulting in continuously extending zigzag-shaped lines. Structural analysis revealed an asymmetric molecular arrangement in the trimer, and suggested that at least four different interactions between neighbouring protomers are involved. A combination of such multiple interactions would be important for linear strand formation of membrane proteins in a lipid bilayer.

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The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat

Abstract

Bibliographical note

ASJC Scopus subject areas

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