Skip Navigation

Journal of Biochemistry 2006 139(5):887-901; doi:10.1093/jb/mvj096
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Kuwana, R.
Right arrow Articles by Watabe, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kuwana, R.
Right arrow Articles by Watabe, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

Regular Paper

Modification of GerQ Reveals a Functional Relationship between Tgl and YabG in the Coat of Bacillus subtilis Spores

Ritsuko Kuwana, Naoyuki Okuda, Hiromu Takamatsu* and Kazuhito Watabe

Faculty of Pharmaceutical Sciences, Setsunan University, Hirakata, Osaka 573-0101

* To whom correspondence should be addressed. Tel/Fax: +81-72-866-3114, E-mail: takamatu{at}pharm.setsunan.ac.jp

Here we describe the functional relationship between YabG and transglutaminase (Tgl), enzymes that modify the spore coat proteins of Bacillus subtilis. In wild-type spores at 37°C, Tgl mediates the crosslinking of GerQ into higher molecular mass forms; however, some GerQ multimers are found in tgl mutant spores, indicating that Tgl is not essential. Immunoblotting showed that spores isolated from a yabG mutant after sporulation at 37°C contain only very low levels of GerQ multimers. Heat treatment for 20 min at 60°C, which maximally activates the enzymatic activity of Tgl, 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°C was lower than that of wild-type spores. These findings suggest that Tgl cooperates with YabG to mediate the temperature-dependent modification of the coat proteins, a process associated with spore germination in B. subtilis.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
R. Kuwana, H. Takamatsu, and K. Watabe
Expression, Localization and Modification of YxeE Spore Coat Protein in Bacillus subtilis
J. Biochem., December 1, 2007; 142(6): 681 - 689.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
A. Masayama, R. Kuwana, H. Takamatsu, H. Hemmi, T. Yoshimura, K. Watabe, and R. Moriyama
A Novel Lipolytic Enzyme, YcsK (LipC), Located in the Spore Coat of Bacillus subtilis, Is Involved in Spore Germination
J. Bacteriol., March 15, 2007; 189(6): 2369 - 2375.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
A. Monroe and P. Setlow
Localization of the Transglutaminase Cross-Linking Sites in the Bacillus subtilis Spore Coat Protein GerQ
J. Bacteriol., November 1, 2006; 188(21): 7609 - 7616.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.