Open Accessɛ‐(γ‐Glutamyl)lysine cross‐links of spore coat proteins and transglutaminase activity in Bacillus subtilis
Author(s) -
Kobayashi Katsunori,
Kumazawa Yoshiyuki,
Miwa Kiyoshi,
Yamanaka Shigeru
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08523.x
Subject(s) - bacillus subtilis , spore , dithiothreitol , lysine , tissue transglutaminase , biochemistry , enzyme , biology , proteolytic enzymes , protease , chemistry , microbiology and biotechnology , amino acid , bacteria , genetics
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 ɛ‐(γ‐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 ɛ‐(γ‐glutamyl)lysine bonds between spore coat proteins.