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 () and Sachiko Tsukita ()
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Hiroshi Suzuki: Cellular and Structural Physiology Institute (CeSPI), Nagoya University
Yasuyuki Ito: Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University
Yuji Yamazaki: Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University
Katsuhiko Mineta: Graduate School of Information Science and Technology, Hokkaido University, Kita, Sapporo
Masami Uji: Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University
Kazuhiro Abe: Cellular and Structural Physiology Institute (CeSPI), Nagoya University
Kazutoshi Tani: Cellular and Structural Physiology Institute (CeSPI), Nagoya University
Yoshinori Fujiyoshi: Cellular and Structural Physiology Institute (CeSPI), Nagoya University
Sachiko Tsukita: Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms2731

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