SUMMARY: The structural gene () encoding the ammonia-assimilation enzyme glutamine synthetase (GS) has been cloned from the obligate methanotroph (Bath). Complementation of mutants was demonstrated. expression analysis revealed that the cloned gene coded for a polypeptide of apparent 60000, as determined by PAGE. Expression of the (Bath) gene in was regulated by nitrogen levels in an Ntr but not an Ntr background. The nucleotide sequence of the (Bath) gene and flanking sequences was determined. This gene, of 1407 bp, encoded a polypeptide of 51717 containing 468 amino acids. The 5’ leader region contained three putative promoters. Promoters P and P resembled the canonical - 10 - 35 -type promoter. Promoter P, which was located between P and P, resembled the NtrA-dependent promoters of enteric organisms. A potential NtrC-binding site was also determined, flanking the Pribnow box at P. Comparisons of nucleotide-derived amino acid sequences of GS enzymes from prokaryotes and eukaryotes with GS from are made.


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