酵母 Sup35 在不同区域的聚集序列促进了脱辅基肌红蛋白的原纤维形成。

Fibrillogenesis of apomyoglobin facilitated by aggregation sequence of yeast Sup35 in various regions.

作者信息

He Yingbo, Tang Huadong, Yi Zhiwei, Zhou Hao, Luo Yongzhang

机构信息

Laboratory of Protein Chemistry, MOE Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, PR China.

出版信息

FEBS Lett. 2005 Feb 28;579(6):1503-8. doi: 10.1016/j.febslet.2005.01.059.

DOI:10.1016/j.febslet.2005.01.059

PMID:15733864

Abstract

To examine the effect of aggregation sequence QGGYQQQYNP from yeast Sup35 on fibril formation of sperm whale apomyoglobin (apoMb), we constructed several mutants via substitution. Urea-induced unfolding of apoMb confirms that the substitution of the aggregation sequence does not significantly affect the stability of the mutants compared to wild type (WT) at pH 4.2. Under this condition, however, despite the difference in rate most apoMb mutants form fibrils more readily than WT with distinct morphology. These results suggest that the aggregation sequence facilitates fibril assembly of apoMb at acidic pH in vitro and this facilitation depends on the regions replaced.

摘要

为了研究酵母 Sup35 的聚集序列 QGGYQQQYNP 对抹香鲸脱辅基肌红蛋白（apoMb）纤维形成的影响，我们通过替换构建了几个突变体。尿素诱导的 apoMb 解折叠证实，与野生型（WT）相比，在 pH 4.2 时聚集序列的替换对突变体的稳定性没有显著影响。然而，在这种条件下，尽管速率有所不同，但大多数 apoMb 突变体比 WT 更容易形成具有独特形态的纤维。这些结果表明，聚集序列在体外酸性 pH 条件下促进了 apoMb 的纤维组装，并且这种促进作用取决于被替换的区域。