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Structural characterization of the mechanosensitive channel candidate MCA2 from Arabidopsis thaliana.


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.

SUBMITTER: Shigematsu H 

PROVIDER: S-EPMC3903776 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Structural characterization of the mechanosensitive channel candidate MCA2 from Arabidopsis thaliana.

Shigematsu Hideki H   Iida Kazuko K   Nakano Masataka M   Chaudhuri Pratima P   Iida Hidetoshi H   Nagayama Kuniaki K  

PloS one 20140127 1


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  ...[more]

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