PRIMARY STRUCTURE OF BARWIN - A BARLEY SEED PROTEIN CLOSELY RELATED TO THE C-TERMINAL DOMAIN OF PROTEINS ENCODED BY WOUND-INDUCED PLANT GENES
PRIMARY STRUCTURE OF BARWIN - A BARLEY SEED PROTEIN CLOSELY RELATED TO THE C-TERMINAL DOMAIN OF PROTEINS ENCODED BY WOUND-INDUCED PLANT GENES
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DOI：
10.1021/bi00152a012
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发表时间：
1992-09-22
期刊：
影响因子：
2.9
通讯作者：
POULSEN, FM
中科院分区：
文献类型：
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作者：
SVENSSON, B;SVENDSEN, I;POULSEN, FM
Barwin蛋白是从大麦种子水提取物中分离出来的碱性蛋白，pI大于10，分子量为13.7 kDa。125个残基的完整氨基酸序列已通过常规蛋白质测序，等离子解吸质谱和H-1核磁共振谱的组合确定。用H-1核磁共振谱和等离子体解吸质谱测定了3个二硫桥分别为Cys31-Cys63、Cys52-Cys86和Cys66-Cys123。n端残基鉴定为焦谷氨酸。Barwin与马铃薯中两个损伤诱导基因win1和win2编码的蛋白c端122个残基的肽段以及橡胶树hevein基因编码的蛋白密切相关。在125个barwin、win1、win2和hevein蛋白序列的77个序列位置中，当在barwin序列中引入两个间隙（允许插入Gly23和Ala24的两个残基中的一个和允许插入Thr97的一个）时，它们具有氨基酸序列同源性。与马铃薯和橡胶树基因编码的蛋白质序列相似，以及该蛋白质结合糖类的能力表明，barwin可能属于一组参与植物共同防御机制的蛋白质。
Barwin is a basic protein with pI above 10 and molecular mass 13.7 kDa isolated from aqueous extracts of barley seed. The complete amino acid sequence of 125 residues has been determined by a combination of conventional protein sequencing, plasma desorption mass spectrometry, and H-1 nuclear magnetic resonance spectroscopy. Three disulfide bridges have been localized as Cys31-Cys63, Cys52-Cys86, and Cys66-Cys123 both by H-1 nuclear magnetic resonance spectroscopy and by plasma desorption mass spectrometry. The N-terminal residue was identified as pyroglutamate. Barwin is closely related to a peptide segment of 122 residues at the C-terminal region of the proteins encoded by two wound-induced genes in potato plants, win1 and win2, and a protein encoded by the hevein gene of rubber tree. In 77 sequence positions of 125 the barwin, win1, win2, and hevein protein sequences have amino acid sequence identity, when two gaps-one of two residues allowing for the insert of Gly23 and Ala24 and one allowing for the insert of Thr97 in the barwin sequence-are introduced in the latter three. The close sequence similarity with the proteins encoded by the wound-induced potato and rubber tree genes and the ability of the protein to bind saccharides suggest that barwin might belong to a group of proteins involved in a common defense mechanism in plants.