Glutamine synthetase in Bacteroides fragilis

Bactereroides fragilis is a gram-negative, non spore-forming, obligate anaerobe of the human intestinal microbiota. It is, however, an opportunistic pathogen and has been ranked as the most prevalent isolate in cases of anaerobic septicaemia. Similar to most bacteria, ammonium is assimilated in B. fragilis through the action of glutamine synthetase (GS). Glutamine is vital to nitrogen metabolism as it serves as a precursor to many secondary metabolites. GS enzymes are, therefore, vital to the growth of the organism and many prokaryotes are known to possess two or more isoforms of the enzyme. In addition, GS expression and regulation is usually tightly regulated in concert with the availability of nitrogen. Previous studies have identified a single GSIII encoding gene (glnN) in B. fragilis. In this dissertation, an additional ORF coding for a putative GSI enzyme in B. fragilis was identified, isolated and functionally characterized. A putative regulatory protein was also identified and its functional contribution to nitrogen metabolism was determined, in order to extend our understanding of nitrogen assimilation in B. fragilis.

Grantor dc:publisher.institution

Department of Molecular and Cell Biology

Year dc:date.issued

2007

Author dc:creator

• Tumba, Nancy

Advisor dc:contributor.advisor

• Abratt, Valerie Rose

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/11427/14720

OAI identifier oai:identifier

oai:open.uct.ac.za:11427/14720