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TitleStructural characterization of the mechanosensitive channel candidate MCA2 from Arabidopsis thaliana.
Journal, issue, pagesPLoS One, Vol. 9, Issue 1, Page e87724, Year 2014
Publish dateJan 27, 2014
AuthorsHideki Shigematsu / Kazuko Iida / Masataka Nakano / Pratima Chaudhuri / Hidetoshi Iida / Kuniaki Nagayama /
PubMed AbstractMechanosensing in plants is thought to be governed by sensory complexes containing a Ca²⁺-permeable, mechanosensitive channel. The plasma membrane protein MCA1 and its paralog MCA2 from ...Mechanosensing in plants is thought to be governed by sensory complexes containing a Ca²⁺-permeable, mechanosensitive channel. The plasma membrane protein MCA1 and its paralog MCA2 from Arabidopsis thaliana are involved in mechanical stress-induced Ca²⁺ influx and are thus considered as candidates for such channels or their regulators. Both MCA1 and MCA2 were functionally expressed in Sf9 cells using a baculovirus system in order to elucidate their molecular natures. Because of the abundance of protein in these cells, MCA2 was chosen for purification. Purified MCA2 in a detergent-solubilized state formed a tetramer, which was confirmed by chemical cross-linking. Single-particle analysis of cryo-electron microscope images was performed to depict the overall shape of the purified protein. The three-dimensional structure of MCA2 was reconstructed at a resolution of 26 Å from 5,500 particles and appears to comprise a small transmembrane region and large cytoplasmic region.
External linksPLoS One / PubMed:24475319 / PubMed Central
MethodsEM (single particle)
Resolution26.0 Å
Structure data

EMDB-2313:
3D reconstruction of Mechanosensitive Channel Candidate MCA2
Method: EM (single particle) / Resolution: 26.0 Å

Source
  • Arabidopsis thaliana (thale cress)

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