@article{10.1371/journal.pone.0087724, doi = {10.1371/journal.pone.0087724}, author = {Shigematsu, Hideki AND Iida, Kazuko AND Nakano, Masataka AND Chaudhuri, Pratima AND Iida, Hidetoshi AND Nagayama, Kuniaki}, journal = {PLOS ONE}, publisher = {Public Library of Science}, title = {Structural Characterization of the Mechanosensitive Channel Candidate MCA2 from Arabidopsis thaliana}, year = {2014}, month = {01}, volume = {9}, url = {https://doi.org/10.1371/journal.pone.0087724}, pages = {1-9}, abstract = {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.}, number = {1}, }