Affiliation:
1. Department of Microbiology, University of Cape Town, Rondebosch 7700, South Africa
Abstract
A glutamine synthetase (GS) gene,
glnA
, from the gram-positive obligate anaerobe
Clostridium acetobutylicum
was cloned on recombinant plasmid pHZ200 and enabled
Escherichia coli glnA
deletion mutants to utilize (NH
4
)
2
SO
4
as a sole source of nitrogen. The cloned
C. acetobutylicum
gene was expressed from a regulatory region contained within the cloned DNA fragment.
glnA
expression was subject to nitrogen regulation in
E. coli
. This cloned
glnA
DNA did not enable an
E. coli glnA ntrB ntrC
deletion mutant to utilize arginine or low levels of glutamine as sole nitrogen sources, and failed to activate histidase activity in this strain which contained the
Klebsiella aerogenes hut
operon. The GS produced by pHZ200 was purified and had an apparent subunit molecular weight of approximately 59,000. There was no DNA or protein homology between the cloned
C. acetobutylicum glnA
gene and GS and the corresponding gene and GS from
E. coli
. The
C. acetobutylicum
GS was inhibited by Mg
2+
in the γ-glutamyl transferase assay, but there was no evidence that the GS was adenylylated.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
29 articles.
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