Molecular Analysis of a Novel Glutamine Synthetase of the Anaerobe Bacteroides fragilis

Hill, Russell T.; Parker, John; Goodman, Heide J. K.; Jones, David T.; Woods, David R.

doi:10.1099/00221287-135-12-3271

Cited by 47 publications

(34 citation statements)

References 31 publications

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“…(Rochefort and Benson 1990) has led to speculation that the two gene variants are the result of an early gene duplication which preceded the divergence of prokaryotes and eukaryotes (Kumada et al 1993). Genes for GSIII, a third type of glutamine synthetase, have recently been sequenced in Bacteroides fragilis (Hill et al 1988), Rhizobium leguminosarum (Chiurazzi et al 1992), and Butyrivibrio fibrisolvens (Goodman and Woods 1993).…”

Section: Introductionmentioning

confidence: 99%

Evolutionary relationships of bacterial and archaeal glutamine synthetase genes

et al. 1994

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Glutamine synthetase (GS), an essential enzyme in ammonia assimilation and glutamine biosynthesis, has three distinctive types: GSI, GSII and GSIII. Genes for GSI have been found only in bacteria (eubacteria) and archaea (archaebacteria), while GSII genes only occur in eukaryotes and a few soil-dwelling bacteria. GSIII genes have been found in only a few bacterial species. Recently, it has been suggested that several lateral gene transfers of archaeal GSI genes to bacteria may have occurred. In order to study the evolution of GS, we cloned and sequenced GSI genes from two divergent archaeal species: the extreme thermophile Pyrococcus furiosus and the extreme halophile Haloferax volcanii. Our phylogenetic analysis, which included most available GS sequences, revealed two significant prokaryotic GSI subdivisions: GSI-alpha and GSI-beta. GSI-alpha-genes are found in the thermophilic bacterium, Thermotoga maritima, the low G+C Gram-positive bacteria, and the Euryarchaeota (includes methanogens, halophiles, and some thermophiles). GSI-beta-type genes occur in all other bacteria. GSI-alpha- and GSI-beta-type genes also differ with respect to a specific 25-amino-acid insertion and adenylylation control of GS enzyme activity, both absent in the former but present in the latter. Cyanobacterial genes lack adenylylation regulation of GS and may have secondarily lost it. The GSI gene of Sulfolobus solfataricus, a member of the Crenarchaeota (extreme thermophiles), is exceptional and could not be definitely placed in either subdivision.

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Section: Introductionmentioning

confidence: 99%

Evolutionary relationships of bacterial and archaeal glutamine synthetase genes

et al. 1994

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“…An apparent molecular weight (Mr) of the putative mature HI-9 was calculated to be 75,720, well coinciding with Mr about 75,000 reported for GSIII from prokaryotes (Hill et al, 1989). Based on these results, HI-9 was defined as diatom GSIII (dGSIII).…”

Section: Full-length Cdna Cloning and Sequence Analysismentioning

confidence: 99%

“…On the other hand, GSIII, initially identified in an anaerobic bacterium Bacteroides fragilis that grows in mammalian intestines (Hill et al, 1989), is composed of six identical subunits each of Mr about 75,000 with little homology to GSI and GSII. GSIII was the most recently discovered family among GSs and thus has been described from a limited number of bacteria including a few cyanobacteria, but not from eukaryotes.…”

Section: Introductionmentioning

confidence: 99%

The occurrence of eukaryotic type III glutamine synthetase in the marine diatom Chaetoceros compressum

Kinoshita¹,

Isu²,

Kaneko³

et al. 2009

Marine Genomics

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“…The structure of both the B. fragilis glnA promoter and coding regions has very little similarity to the well-characterized glnA gene from E. coli (Hill et al 1989). It is, therefore, possible that the regulation of the B. fragilis glnA gene could also be novel and could involve transcriptional, translational, or post-translational events.…”

Section: Introductionmentioning

confidence: 95%

“…The B. fragilis glnA gene has been cloned, sequenced and characterized (Southern et al 1986(Southern et al , 1987Hill et al 1989) and shown to code for a structurally novel glutamine synthetase (GSIII) enzyme. The gene is regulated in B. fragilis by ammonia at the level of transcription (Abratt et al 1993), but details of the molecular mechanisms, recognition sequences, or other genes that might be involved in transcription and translation are not known.…”

Section: Introductionmentioning

confidence: 99%

Cloning of an EF-P homologue from Bacteroides fragilis that increases B. fragilis glutamine synthetase activity in Escherichia coli

Abratt

Mbewe²,

Woods

1998

Mol Gen Genet

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Investigations of possible regulators of Bacteroides fragilis glutamine synthetase (GS) activity were done in Escherichia coli using a compatible dual-plasmid system. The B. fragilis glnA gene, together with upstream and downstream flanking regions, was cloned onto the low copy number plasmid pACYC184 and expressed in the E. coli glnA ntrB ntrC deletion strain, YMC11. GS activity was monitored following co-transformation with a B. fragilis genomic library carried on the compatible plasmid pEcoR251. A gene was cloned that caused a twofold increase in B. fragilis GS activity but did not affect the activity of the E. coli GS enzyme or the B. fragilis sucrase (ScrL). Deletion of the B. fragilis glnA downstream region decreased basal levels of GS activity, but did not affect the ability of the cloned gene to increase the B. fragilis GS activity. Reporter gene analysis, using the B. fragilis glnA promoter region fused to the promoterless Clostridium acetobutylicum endoglucanase gene, showed no increase in reporter gene activity. This demonstrated that the increase in GS activity was not regulated at the transcriptional level, and that the cloned gene product was not affecting the copy number of the plasmid in trans. Sequence data indicated that the cloned gene had good amino acid identity to a range of elongation factor P (EF-P) proteins, the highest being to that of a Synechocystis sp (48%), and the least to Mycobacterium genitalium (27%). Amino acid identity to the E. coli EF-P was intermediate (37%). A possible role for EF-P in enhancing translation of the B. fragilis glnA mRNA is proposed.

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Molecular Analysis of a Novel Glutamine Synthetase of the Anaerobe Bacteroides fragilis

Cited by 47 publications

References 31 publications

Evolutionary relationships of bacterial and archaeal glutamine synthetase genes

Evolutionary relationships of bacterial and archaeal glutamine synthetase genes

The occurrence of eukaryotic type III glutamine synthetase in the marine diatom Chaetoceros compressum

Cloning of an EF-P homologue from Bacteroides fragilis that increases B. fragilis glutamine synthetase activity in Escherichia coli

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