The basidiomycete Ustilago maydis has two plasma membrane H⁺-ATPases related to fungi and plants.
The basidiomycete Ustilago maydis has two plasma membrane H⁺-ATPases related to fungi and plants.
复制标题
担子菌Ustilago maydis有两种与真菌和植物相关的质膜H+-ATP酶。
DOI：
10.1007/s10863-013-9520-1
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发表时间：
2013
影响因子：
3
通讯作者：
Guerra-Sánchez,Guadalupe
中科院分区：
文献类型：
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作者：
Robles-Martínez,Leobarda;Pardo,JuanPablo;Miranda,Manuel;Mendez,TavisL;Matus-Ortega,MacarioGenaro;Mendoza-Hernández,Guillermo;Guerra-Sánchez,Guadalupe
真菌和植物的质膜H+- atp酶在酵母、植物和原生动物细胞的生理中起着重要的作用。在担子菌黑穗病菌（ustilago maydis）中鉴定出两个编码质膜H+- atp酶的基因，其中一个与真菌（um02581）和植物（um01205） H+- atp酶具有较高的同源性。与在富含YPD的培养基中培养的细胞相比，在少量乙醇培养基中培养的细胞质子泵活性高5倍，但两种条件下总钒酸盐敏感atp酶活性相同。相比之下，在葡萄糖培养基中培养的细胞的活性比在YPD或乙醇培养基中培养的细胞高2倍，这暗示了细胞质膜atp酶活性的调节机制。对不同生长条件下细胞中H+-ATPases的基因表达分析表明，植物型的um01205转录本的表达量高于真菌型的um02581。质谱分析证实了这两个蛋白的翻译作用。与面包酵母和植物H+- atp酶不同，它们的活性分别通过与葡萄糖或蔗糖短暂孵育而增加。可能dish +- atp酶活性在这些糖的作用下没有改变。两个ou的序列分析。许多dish +- atp酶显示，酿酒酵母和拟南芥细胞膜H+- atp酶缺乏作为蛋白激酶靶点的典型苏氨酸和丝氨酸残基，这表明u +- atp酶的磷酸化。五月解酶发生在不同的氨基酸残基上。
The fungal and plant plasma membrane H+-ATPases play critical roles in the physiology of yeast, plant and protozoa cells. We identified two genes encoding two plasma membrane H+-ATPases in the basidiomyceteUstilago maydis, one protein with higher identity to fungal (um02581) and the other to plant (um01205) H+-ATPases. Proton pumping activity was 5-fold higher when cells were grown in minimal medium with ethanol compared to cells cultured in rich YPD medium, but total vanadate-sensitive ATPase activity was the same in both conditions. In contrast, the activity in cells cultured in minimal medium with glucose was 2-fold higher than in YPD or ethanol, implicating mechanisms for the regulation of the plasma membrane ATPase activity inU.maydis. Analysis of gene expression of the H+-ATPases from cells grown under different conditions, showed that the transcript expression ofum01205(plant-type) was higher than that ofum02581(fungal-type). The translation of the two proteins was confirmed by mass spectrometry analysis. Unlike baker’s yeast and plant H+-ATPases, where the activity is increased by a short incubation with glucose or sucrose, respectively,U.maydisH+-ATPase activity did not change in response to these sugars. Sequence analysis of the twoU.maydisH+-ATPases revealed the lack of canonical threonine and serine residues which are targets of protein kinases inSaccharomyces cerevisiaeandArabidopsis thalianaplasma membrane H+-ATPases, suggesting that phosphorylation of theU. maydisenzymes occurs at different amino acid residues.