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Journal of Bacteriology, October 2001, p. 5826-5833, Vol. 183, No. 20
Department of Genetics, The University of
Melbourne, Parkville, Victoria, 3010, Australia,1 Department of Genetics, Duke
University Medical Center, Durham, North Carolina
27710,2 and Monsanto, Mystic,
Connecticut 063553
Received 23 March 2001/Accepted 16 June 2001
Glutamine synthetase (GS), EC 6.3.1.2, is a central enzyme in the
assimilation of nitrogen and the biosynthesis of glutamine. We have
isolated the Aspergillus nidulans glnA gene encoding GS and
have shown that glnA encodes a highly expressed but not
highly regulated mRNA. Inactivation of glnA results in
an absolute glutamine requirement, indicating that GS is responsible
for the synthesis of this essential amino acid. Even when supplemented
with high levels of glutamine, strains lacking a functional
glnA gene have an inhibited morphology, and a wide range of
compounds have been shown to interfere with repair of the glutamine
auxotrophy. Heterologous expression of the prokaryotic Anabaena
glnA gene from the A. nidulans alcA promoter allowed
full complementation of the A. nidulans glnA
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.20.5826-5833.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Role of Glutamine Synthetase in Nitrogen Metabolite
Repression in Aspergillus nidulans
mutation.
However, the A. nidulans fluG gene, which encodes a protein
with similarity to prokaryotic GS, did not replace A. nidulans
glnA function when similarly expressed. Our studies with the
glnA
mutant confirm that glutamine, and not GS, is the
key effector of nitrogen metabolite repression. Additionally, ammonium and its immediate product glutamate may also act directly to signal nitrogen sufficiency.
*
Corresponding author. Mailing address: Department of
Genetics, The University of Melbourne, Parkville, Victoria, 3010, Australia. Phone: 613 8344 6246. Fax: 613 8344 5139. E-mail:
m.davis{at}genetics.unimelb.edu.au.
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