The fission yeast synaptobrevin ortholog Syb1 plays an important role in forespore membrane formation and spore maturation.
The fission yeast synaptobrevin ortholog Syb1 plays an important role in forespore membrane formation and spore maturation.
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裂殖酵母突触短蛋白直系同源物 Syb1 在前孢子膜形成和孢子成熟中发挥重要作用。
DOI:
10.1128/ec.00061-13
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发表时间:
2013
期刊:
影响因子:
--
通讯作者:
Taro Nakamura (T. Y. and K. I. contributed equally to this article)
中科院分区:
文献类型:
--
作者:
Tomomi Yamaoka;Kazuki Imada;Kana Fukunishi;Yuriko Yamasaki;Chikashi Shimoda;Taro Nakamura (T. Y. and K. I. contributed equally to this article)
Synaptobrevin, also called vesicle-associated membrane protein (VAMP), is a component of the plasma membrane N-methylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, which plays a key role in intracellular membrane fusion. Previous studies have revealed that, similar to synaptobrevin in other organisms, the fission yeast synaptobrevin ortholog Syb1 associates with post-Golgi secretory vesicles and is essential for cytokinesis and cell elongation. Here, we report that Syb1 has a role in sporulation. After nitrogen starvation, green fluorescent protein (GFP)-Syb1 is found in intracellular dots. As meiosis proceeds, GFP-Syb1 accumulates around the nucleus and then localizes at the forespore membrane (FSM). We isolated asyb-S1mutant, which exhibits a defect in sporulation. Insyb1-S1mutants, the FSM begins to form but fails to develop a normal morphology. Electron microscopy shows that an abnormal spore wall is often formed insyb1-S1mutant spores. Although mostsyb1-S1mutant spores are germinated, they are less tolerant to ethanol than wild-type spores. Thesyb1-S1allele carries a missense mutation, resulting in replacement of a conserved cysteine residue adjacent to the transmembrane domain, which reduces the stability and abundance of the Syb1 protein. Taken together, these results indicate that Syb1 plays an important role in both FSM assembly and spore wall formation.