epsilon-(gamma Glutamyl)lysine cross-links of spore coat proteins and transglutaminase activity in Bacillus subtilis

被引：57

作者：

Kobayashi, K ^{[1
]}

Kumazawa, Y ^{[1
]}

Miwa, K ^{[1
]}

Yamanaka, S ^{[1
]}

机构：

[1] AJINOMOTO CO INC,FOOD RES & DEV LABS,KAWASAKI KU,KAWASAKI,KANAGAWA 210,JAPAN

来源：

FEMS MICROBIOLOGY LETTERS | 1996年 / 144卷 / 2-3期

关键词：

Bacillus subtilis; epsilon-(gamma-glutamyl)lysine; transglutaminase; spore coat;

D O I：

10.1016/0378-1097(96)00353-9

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Spores of Bacillus subtilis are resistant to proteolytic enzymes. Some of the spore coat proteins cannot be solubilized even by treatment with strong chemical agents like dithiothreitol. The spore coat has been suggested to possess cross-links between proteins in addition to disulfide bonds. We analyzed B. subtilis spore coat proteins to find specific cross-link structures. We detected epsilon-(gamma-glutamyl)lysine in the spore coat proteins after sequential protease digestion followed by HPLC. We also detected transglutaminase activity in sporulating cells, which incorporated putrescine into N,N'-dimethylcasein. This enzyme was suggested to create epsilon-(gamma-glutamyl)lysine bonds between spore coat proteins.

引用

页码：157 / 160

页数：4

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