Characterization of two genes, glpQ and ugpQ, encoding glycerophosphoryl diester phosphodiesterases of Escherichia coli

✍ Scribed by Tommassen, Jan ;Eiglmeier, Karin ;Cole, Stewart T. ;Overduin, Piet ;Larson, Timothy J. ;Boos, Winfried

• Book ID: 104697082
• Publisher: Springer
• Year: 1991
• Tongue: English
• Weight: 834 KB
• Volume: 226-226
• Category: Article
• ISSN: 0026-8925
• DOI: 10.1007/bf00273621

✦ Synopsis

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.