AtCAX1 N-terminal can improve Ca2+ and Ba2+ tolerance in yeast
1. Key Laboratory of Saline-alkali Vegetation Ecology Restoration in Oil Field (SAVER), Ministry of Education, Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin, 150040
2. Asian Natural Environmental Science Center (ANESC), The University of Tokyo, Nishi-tokyo-shi, Tokyo, Japan
Cell Biology and Biophysics, 2015, Vol. 4, No. 3 doi: 10.5376/cbb.2015.04.0003
Received: 08 Jun., 2015 Accepted: 23 Jun., 2015 Published: 29 Jun., 2015
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Preferred citation for this article:
Hongjun Guo, Daisuke Tsugama, Tetsuo Takano, Yuanyuan Bu and Shenkui Liu, 2015, AtCAX1 N-terminal may enhance Ca2+ and Ba2+ tolerance in yeast, Cell Biology and Biophysics, 4(3): 1-4 (doi: 10.5376/cbb.2015.04.0003)
AtCAX1 is a member of the Ca2+/H+ antiporter family. The N-terminally truncated AtCAX1 (ΔN108AtCAX1) and the C-terminally segment truncated AtCAX1 (ΔC9AtCAX1, ΔC36AtCAX1, and ΔC144AtCAX) and full-length AtCAX1 were created and analyzed their growth in the presence of Ba2+ and Ca2+. The ΔN108AtCAX1 grew well in the presence of 150 mM Ca2+ and 15mM Ba2+. This result indicates that ΔN108AtCAX1 can improve the resistance to Ca2+ and Ba2+. And by atomic absorption spectrophotometer to measure the Ba2+ content of whole yeast cells, the results showed that the Ba2+ content in yeast cell expressing ΔN108AtCAX1 was lower than other yeast transformants. The studies indicate that AtCAX1 may transport Ca2+ and Ba2+.
AtCAX1; Ca2+ and Ba2+ tolerance; Auto-inhibitory domain
Cell Biology and Biophysics
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