Heat stable ssDNA/RNA-binding activity of a wheat cold shock domain protein
Heat stable ssDNA/RNA-binding activity of a wheat cold shock domain protein
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DOI：
10.1016/j.febslet.2005.07.074
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发表时间：
2005-08-29
期刊：
影响因子：
3.5
通讯作者：
Imai, R
中科院分区：
文献类型：
--
作者：
Nakaminami, K;Sasaki, K;Imai, R
冷诱导小麦WCSPI蛋白属于冷激激域蛋白家族。在原核生物和真核生物中，CSD作为一个核酸结合域发挥作用。在这里，我们证明了纯化的重组WCSPI是沸腾可溶的，并结合了ss/dsDNA和mRNA。此外，煮熟的WCSP1保留了其特有的核酸结合活性。只含有CSD的WCSPI缺失突变体失去了单链DNA/RNA结合活性，而包含CSD和第一甘氨酸富集区(GR)的突变体显示了这种活性。这些数据表明，WCSPI的第一个GR是结合活性所必需的，但对蛋白质的热稳定性不是必需的。(C)2005年欧洲生化学会联合会。爱思唯尔出版，版权所有。
The cold-induced wheat WCSPI protein belongs to the cold shock domain (CSD) protein family. In prokaryotes and eukaryotes, the CSD functions as a nucleic acid-binding domain. Here, we demonstrated that purified recombinant WCSPI is boiling soluble and binds ss/dsDNA and mRNA. Furthermore, boiled-WCSP1 retained its characteristic nucleic acid-binding activity. A WCSPI deletion mutant, containing only a CSD, lost ssDNA/RNA-binding activity; while a mutant containing the CSD and the first glycine-rich region (GR) displayed the activity. These data indicated that the first GR of WCSPI is necessary for the binding activity but is not for the heat stability of the protein. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.