PMID:1851953
| Citation |
Tommassen, J, Eiglmeier, K, Cole, ST, Overduin, P, Larson, TJ and Boos, W (1991) Characterization of two genes, glpQ and ugpQ, encoding glycerophosphoryl diester phosphodiesterases of Escherichia coli. Mol. Gen. Genet. 226:321-7 |
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| Abstract |
The nucleotide sequences of the glpQ and ugpQ genes of Escherichia coli, which both encode glycerophosphoryl diester phosphodiesterases, were determined. The glpQ gene encodes a periplasmic enzyme of 333 amino acids, produced initially with a 25 residue long signal sequence, while ugpQ codes for a cytoplasmic protein of 247 amino acids. Despite differences in size and cellular location, significant similarity in the primary structures of the two enzymes was found suggesting a common evolutionary origin. The 3' end of the ugpQ gene overlaps an open reading frame that is transcribed in the opposite direction. This open reading frame encodes a polypeptide with an unusual composition, i.e., 46 of the 146 amino acids are Gln or Asn. This polypeptide and the UgpQ protein were identified in an in vitro transcription/translation system as proteins with apparent molecular weights of 19.5 and 27 kDa, respectively. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA, Bacterial; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Molecular Sequence Data; Open Reading Frames; Phosphoric Diester Hydrolases/genetics; Phosphoric Diester Hydrolases/metabolism; Restriction Mapping; Sequence Alignment |
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