Sequence and molecular analysis of the Rhizobium etli glsA gene, encoding a thermolabile glutaminase.
We sequenced a 2.1 kb fragment of DNA carrying the structural glsA gene, which codes for the Rhizobium etli thermolabile glutaminase (A). The glsA gene complements the R. etli LM16 mutant that lacks glutaminase A activity, and is expressed in the heterologous host Sinorhizobium meliloti. The deduced amino acid sequence consists of 309 residues, with a calculated molecular mass of 33 kDa. The amino acid sequence shares 53% and 43% identity with two hypothetical glutaminases of E. coli; 42% identity with liver-type; 38% identity with kidney-type glutaminase; 41% and 40% identity hypothetical glutaminases of Bacillus subtilis; and 41% and 37% identity with two putative glutaminases of Caenorhabditis elegans. The glsA gene represents the first glutaminase gene cloned and sequenced in prokaryotes.
Calderón
J
J
Instituto de Investigaciones Biomédicas, Departamento de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 70228, C.P. 04510, México, D.F., Mexico.
Huerta-Saquero
A
A
Du Pont
G
G
Durán
S
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D004247:DNA / Q000737:chemistry; D005972:Glutaminase / Q000235:genetics*; D006360:Heat-Shock Proteins / Q000235:genetics; D008969:Molecular Sequence Data; D012231:Rhizobium / Q000201:enzymology / Q000235:genetics*; D016415:Sequence Alignment
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D004247:DNA; C492196:GlsA protein, bacteria; D005972:Glutaminase