Cloning of vacuolar H+-ATPase subunit c genes from Japanese iris, and functional characterization in yeast

被引：1

作者：

Zhou A.-M. ^{[1
]}

Wu D. ^{[1
]}

Che D.-D. ^{[1
]}

Liu S.-K. ^{[2
]}

Yang C.-P. ^{[3
]}

Wang J.-G. ^{[1
,3
]}

机构：

[1] Horticulture college, Northeast Agricultural University

[2] Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University

[3] Key Laboratory of Forest Tree Genetic Improvement and Biotechnology, Ministry of Education, Northeast Forestry University

来源：

Journal of Forestry Research | 2011年 / 22卷 / 3期

关键词：

green fluorescent protein; Japanese iris; subunit c; V-ATPase; yeast;

D O I：

10.1007/s11676-011-0180-x

中图分类号：

学科分类号：

摘要：

Five different isoforms (IrlVHA-c1-c5) of V-ATPase subunit c (VHA-c) were cloned from a Japanese iris (Iris lactea Pall. var. chinensis Fisch. Koidz) cDNA library using degenerate primers PCR and the 5′-RACE technique. The sequence analysis showed the open reading frame (ORF) of the IrlVHA-c1-c5 to be 495 bp, corresponding to a protein of 164 amino acids. Among the five isoforms, IrlVHA-c1 and IrlVHA-c2 are completely homologous. The IrlVHA-c protein is localized at the vacuolar membrane as indicated by a green fluorescent protein (GFP) marker. Its over-expression in yeast could enhance yeast tolerance to NaCl stress. These results show that there are at least five genes encoding different isoforms of IrlVHA-c in Japanese iris and IrlVHA-c is important for the function of V-ATPase. © 2011 Northeast Forestry University and Springer-Verlag Berlin Heidelberg.

引用

页码：361 / 366

页数：5

共 30 条

[1]

Arai H., Terres G., Pink S., Forgac M., Topography and subunit stoichiometry of the coated vesicle proton pump, J Biol Chem, 263, pp. 8796-8802, (1988)

[2]

Brett C.L., Tukaye D.N., Mukherjee S., Rao R., The yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to control vesicle trafficking, Mol Biol Cell, 16, pp. 1396-1405, (2005)

[3]

Cipriano D.J., Wang Y., Bond S., Hinton A., Jefferies K.C., Qi J., Forgac M., Structure and regulation of the vacuolar ATPases, Biochim Biophys Acta, 1777, pp. 599-604, (2008)

[4]

Dietz K.J., Tavakoli N., Kluge C., Mimura T., Sharma S.S., Harris G.C., Chardonnens A.N., Golldack D., Significance of the V-type ATPase for the adaptation to stressful growth conditions and its regulation on the molecular and biochemical level, J Exp Bot, 52, pp. 1969-1980, (2001)

[5]

Drory O., Nelson N., Structural and functional features of yeast V-ATPase subunit C, Biochim Biophys Acta, 1757, pp. 297-303, (2006)

[6]

Ferea T.L., Bowman B.J., The vacuolar ATPase of Neurospora crassa is indispensable: Inactivation of the vma-1 gene in repeat-induced point mutation, Genetics, 143, pp. 147-154, (1996)

[7]

Finbow M.E., Harrison M.A., The vacuolar H+-ATPase: auniversal proton pump of eukaryotes, Biochem J, 324, pp. 697-712, (1997)

[8]

Gietz R.D., Schiestl R.H., Willems A.R., Woods R.A., Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure, Yeast, 11, pp. 355-360, (1995)

[9]

Hasenfratz M.P., Tsou C.L., Wilkins T.A., Expression of two related vacuolar H(+)-ATPase 16-kilodalton proteolipid genes is differentially regulated in a tissue-specific manner, Plant Physiol, 108, pp. 1395-1404, (1995)

[10]

Hilario E., Gogarten J.P., The prokaryote-to-eukaryote transition reflected in the evolution of the V/F/A-ATPase catalytic and proteolipid subunits, J Mol Evol, 46, pp. 703-715, (1998)

← 1 2 3 →