Membrane translocation and insertion of NH2-terminally anchored gamma-glutamyl transpeptidase require a signal recognition particle.
The two subunits of the renal brush border enzyme, gamma-glutamyl transpeptidase (EC 2.3.2.2), are derived from a single-chain propeptide. The membrane-spanning domain consists of a hydrophobic sequence near its NH2-terminus and the protein is oriented with its NH2-terminus on the cytoplasmic side. The enzyme is synthesized without a cleavable signal sequence. Translocation and insertion of this enzyme have been shown to be dependent on the signal recognition particle and presumably require the same translocation machinery that other secretory and membrane proteins use for these processes.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004285:Dogs; D007668:Kidney / Q000201:enzymology*; D008861:Microsomes / Q000201:enzymology; D008871:Microvilli / Q000201:enzymology*; D010179:Pancreas / Q000201:enzymology; D021382:Protein Sorting Signals / Q000502:physiology; D014178:Translocation, Genetic; D005723:gamma-Glutamyltransferase / Q000235:genetics*
D021382:Protein Sorting Signals; D005723:gamma-Glutamyltransferase