Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 150 (2004), 4115-4123; DOI  10.1099/mic.0.27467-0
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
Right arrow Citation Map
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kimura, K.
Right arrow Articles by Itoh, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kimura, K.
Right arrow Articles by Itoh, Y.
Agricola
Right arrow Articles by Kimura, K.
Right arrow Articles by Itoh, Y.
Microbiology 150 (2004), 4115-4123; DOI  10.1099/mic.0.27467-0
© 2004 Society for General Microbiology

Characterization of Bacillus subtilis {gamma}-glutamyltransferase and its involvement in the degradation of capsule poly-{gamma}-glutamate

Keitarou Kimura1, Lam-Son Phan Tran1,{dagger}, Ikuo Uchida2 and Yoshifumi Itoh1,3

1 Division of Applied Microbiology, National Food Research Institute, Kannondai 2-1-12, Tsukuba, Ibaraki 305-8642, Japan
2 Hokkaido Research Station, National Institute of Animal Health, Hitsujigaoka 4, Toyohira-Ku, Sapporo 062-0045, Japan
3 Akita Research Institute of Food and Brewing, Sanuki 4-26, Araya-Machi, Akita 010-1623, Japan

Correspondence
Yoshifumi Itoh
yosifumi{at}arif.pref.akita.jp

During early stationary phase, Bacillus subtilis NAFM5 produces capsular poly({gamma}-glutamic acid) ({gamma}PGA, 2x106 Da), which contains D- and L-glutamate, and then degrades it during late stationary phase. The {gamma}-glutamyltransferase (EC 2.3.2.2; GGT) of this strain successively hydrolysed {gamma}PGA from the amino-terminal end, to yield both D- and L-glutamate. This enzyme was specifically synthesized during the stationary phase through transcriptional activation of the corresponding ggt gene by the ComQXPA quorum-sensing system. A ggt knockout mutant degraded {gamma}PGA into 1x105 Da fragments, but not any further, indicating that the capsule {gamma}PGA is first internally degraded by an endo-type of {gamma}PGA hydrolase into 1x105 Da intermediates, then externally into glutamates via GGT. Due to its inability to generate the glutamates from the capsule, the ggt mutant sporulated more frequently than the wild-type strain. The results show that B. subtilis GGT has a powerful exo-{gamma}-glutamyl hydrolase activity that participates in capsule {gamma}PGA degradation to supply stationary-phase cells with constituent glutamates.

Abbreviations: GGT, {gamma}-glutamyltransferase; {gamma}GNA, {gamma}-glutamyl-p-nitroanilide; {gamma}PGA, poly({gamma}-glutamic acid)

{dagger}Present address: Japan International Research Center for Agricultural Science, Ohwashi 1-1, Tsukuba, Ibaraki 305-8686, Japan.




This article has been cited by other articles:


Home page
 Appl. Environ. Microbiol.Home page
A. Ochiai, T. Itoh, A. Kawamata, W. Hashimoto, and K. Murata
Plant Cell Wall Degradation by Saprophytic Bacillus subtilis Strains: Gene Clusters Responsible for Rhamnogalacturonan Depolymerization
Appl. Envir. Microbiol., June 15, 2007; 73(12): 3803 - 3813.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2004 Society for General Microbiology.