Temperature dependent N-glycosylation of plasma membrane heat shock protein Hsp30p in Saccharomyces cerevisiae
Temperature dependent N-glycosylation of plasma membrane heat shock protein Hsp30p in Saccharomyces cerevisiae
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DOI：
10.1016/j.bbrc.2012.02.126
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发表时间：
2012-03-30
影响因子：
3.1
通讯作者：
Izawa, Shingo
中科院分区：
文献类型：
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作者：
Kamo, Ken'ichi;Takabatake, Akiko;Izawa, Shingo
芽殖酵母酿酒酵母（Saccharomyces cerevisiae）的HSP 30基因编码一种七跨膜热休克蛋白，其表达响应于包括热休克在内的各种类型的应激。虽然Hsp 30 p含有一个潜在的N-糖基化共有序列（Asn（2）-Asp（3）-Thr（4）），但它是否真的被N-糖基化还没有得到证实。在这里，我们证明，N-糖基化诱导的热休克蛋白30 p的Asn（2）的严重热休克，乙醇应激，乙酸应激。轻度热休克和葡萄糖耗竭诱导Hsp 30 p的表达，但不诱导N-糖基化，表明N-糖基化依赖于温度和环境条件。N-糖基化不影响Hsp 3 Op的细胞内定位，但其在严重热休克条件下的生理作用。由于有限的信息是压力响应或条件诱导的N-糖基化，我们的研究结果提供了新的见解酵母细胞应激反应的调节。(C)2012 Elsevier Inc. All rights reserved.
The HSP30 gene of the budding yeast Saccharomyces cerevisiae encodes a seven-transmembrane heat shock protein expressed in response to various types of stress including heat shock. Although Hsp30p contains a potential N-glycosylation consensus sequence (Asn(2)-Asp(3)-Thr(4)), whether it is actually N-glycosylated has not been verified. Here we demonstrate that N-glycosylation is induced at Asn(2) of Hsp30p by severe heat shock, ethanol stress, and acetic acid stress. Mild heat shock and glucose depletion induced the expression but not N-glycosylation of Hsp30p, indicating the N-glycosylation to be dependent on temperature and environmental conditions. N-glycosylation did not affect on the intracellular localization of Hsp3Op but its physiological role under severe heat shock conditions. Since limited information is available on stress-responsive or condition-induced N-glycosylation, our findings provide new insight into the regulation of cellular stress response in yeast. (C) 2012 Elsevier Inc. All rights reserved.