Altered localisation of the precursor of a secreted protein in E. coli by a carboxyl-deletion.
The effect on protein localisation of a carboxy-terminal deletion of periplasmic UDP-glucose hydrolase (5'-nucleotidase) has been determined in vivo using immunoprecipitation. The processed form of the truncated protein was found in the periplasm; however, in contrast to the situation with the normal protein, the preprotein form of the truncated protein was also found in the periplasm. This result confirms previous semi-in vitro data and supports the suggestion that a conformational change in a membrane-bound intermediate is a normal part of the secretory pathway.
Burns
D M
DM
School of Science, Griffith University, Nathan, Brisbane, Qld. Australia.
Beacham
I R
IR
D015720:5'-Nucleotidase; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D005796:Genes; D005815:Genetic Code; D009708:Nucleotidases / Q000235:genetics*; D010957:Plasmids; D011487:Protein Conformation; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D011498:Protein Precursors; D009708:Nucleotidases; D015720:5'-Nucleotidase