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通过来自异源物种的H(+) - ATP酶基因对酵母质膜H(+) - ATP酶基因pma1进行原位互补。

Complementation in situ of the yeast plasma membrane H(+)-ATPase gene pma1 by an H(+)-ATPase gene from a heterologous species.

作者信息

Palmgren M G, Christensen G

机构信息

August Krogh Institute, University of Copenhagen, Denmark.

出版信息

FEBS Lett. 1993 Feb 15;317(3):216-22. doi: 10.1016/0014-5793(93)81279-9.

DOI:10.1016/0014-5793(93)81279-9
PMID:8425607
Abstract

In plants and fungi, the transport of solutes across the plasma membrane (pm) is driven by a proton pump (H(+)-ATPase) that produces an electric potential and a pH gradient. We expressed AHA2, a member of the Arabidopsis thaliana pm H(+)-ATPase gene family, in yeast cells in which transcription of the endogenous pm H(+)-ATPase gene (pma1) had been turned off. AHA2 was expressed mainly in intracellular membranes and only supported very slow growth of transformed yeast cells. Removal of the last 92 C-terminal amino acids from the plant H(+)-ATPase produced an enzyme with 2-3-fold higher specific ATPase activity than the wild-type plant enzyme. Surprisingly, the truncated H(+)-ATPase was now targetted to the yeast pm and fully supported normal yeast growth.

摘要

在植物和真菌中,溶质跨质膜(pm)的运输由质子泵(H(+)-ATP酶)驱动,该质子泵产生电势和pH梯度。我们在已关闭内源性质膜H(+)-ATP酶基因(pma1)转录的酵母细胞中表达了拟南芥质膜H(+)-ATP酶基因家族的成员AHA2。AHA2主要在内膜中表达,仅支持转化酵母细胞非常缓慢的生长。从植物H(+)-ATP酶中去除最后92个C末端氨基酸后产生的一种酶,其比野生型植物酶具有高2至3倍的比ATP酶活性。令人惊讶的是,截短的H(+)-ATP酶现在靶向酵母质膜,并完全支持酵母正常生长。

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