The glutamine synthetase of Prevotella bryantii B(1)4 is a family III enzyme (GinN) and glutamine supports growth of mutants lacking glutamate dehydrogenase activity

Wen, ZT, Peng, LS and Morrison, M (2003) The glutamine synthetase of Prevotella bryantii B(1)4 is a family III enzyme (GinN) and glutamine supports growth of mutants lacking glutamate dehydrogenase activity. Fems Microbiology Letters, 229 1: 15-21. doi:10.1016/S0378-1097(03)00764-X


Author Wen, ZT
Peng, LS
Morrison, M
Title The glutamine synthetase of Prevotella bryantii B(1)4 is a family III enzyme (GinN) and glutamine supports growth of mutants lacking glutamate dehydrogenase activity
Journal name Fems Microbiology Letters   Check publisher's open access policy
ISSN 0378-1097
Publication date 2003-12-01
Year available 2003
Sub-type Article (original research)
DOI 10.1016/S0378-1097(03)00764-X
Open Access Status Not yet assessed
Volume 229
Issue 1
Start page 15
End page 21
Total pages 7
Place of publication AMSTERDAM
Publisher ELSEVIER SCIENCE BV
Language eng
Abstract Prevotella spp. are believed to play a central role in ruminal nitrogen metabolism, but little is understood about the genetics and biochemistry of nitrogen assimilation and regulation in these bacteria. The gene encoding a family III glutamine synthetase (GSIII, glnN) in Prevotella bryantii B(1)4 was cloned by Escherichia coli mutant complementation, and enzyme assays as well as Northern blot analysis showed that maximal enzyme activity and glnN transcription occurred in cells grown under nitrogen-limiting conditions. Addition of methionine sulfoximine (MSX), a GS inhibitor, terminated bacterial growth when ammonium was provided as the sole nitrogen source, but the inhibitory effect could be overcome by the inclusion of either L-glutamine or trypticase in the growth medium. A P. bryantii mutant lacking glutamate dehydrogenase (GdhA) activity was isolated by ethylmethylsulfonate mutagenesis. Growth studies with different nitrogen sources showed that the mutant strain was still capable of growth with ammonium as the sole nitrogen source, albeit at a decreased growth rate. The mutant strain could also grow with L-glutamine as a nitrogen source in the presence of MSX. These data suggest that GlnN provides an effective route of ammonium assimilation for P. bryantii, in addition to that afforded by the glutamate dehydrogenase pathway. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
Keyword Prevotella
Bacteroides
glutamine synthetase
ammonia assimilation
nitrogen regulation
Bacteroides-Fragilis
Ammonia Assimilation
Gdha
Expression
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: ResearcherID Downloads - Archived
 
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