Modification of GerQ reveals a functional relationship between Tgl and YabG in the coat of Bacillus subtilis spores
Modification of GerQ reveals a functional relationship between Tgl and YabG in the coat of Bacillus subtilis spores
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DOI:
10.1093/jb/mvj096
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发表时间:
2006-05-01
影响因子:
2.7
通讯作者:
Watabe, Kazuhito
中科院分区:
文献类型:
--
作者:
Kuwana, Ritsuko;Okuda, Naoyuki;Watabe, Kazuhito
Here we describe the functional relationship between YabG and transglutaminase (Tg1), enzymes that modify the spore coat proteins of Bacillus subtilis. In wild-type spores at 37 degrees C, Tg1 mediates the crosslinking of GerQ into higher molecular mass forms; however, some GerQ multimers are found in tg1 mutant spores, indicating that Tg1 is not essential. Immunoblotting showed that spores isolated from a yabG mutant after sporulation at 37 degrees C contain only very low levels of GerQ multimers. Heat treatment for 20 min at 60 degrees C, which maximally activates the enzymatic activity of Tg1, caused crosslinking of GerQ in isolated yabG spores but not in tgl/yabG double-mutant spores. In addition, the germination frequency of the tgl/yabG spores in the presence of L-alanine with or without heat activation at 60 degrees C was lower than that of wild-type spores. These findings suggest that Tg1 cooperates with YabG to mediate the temperature-dependent modification of the coat proteins, a process associated with spore germination in B. subtilis.