Forskning ved Københavns Universitet - Københavns Universitet


Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

From a genomic library of Serratia liquefaciens, a cloned DNA fragment comprising a two-gene operon was isolated and expressed in Escherichia coli. One of the gene products was identified as a phospholipase A1, and the enzyme was found to be excreted to the outer environment from S. liquefaciens as well as from E. coli. Both genes were sequenced, and the relationship between open reading frames in the DNA sequence and in vitro-expressed polypeptides was established. The length of the phospholipase polypeptide was found to be 319 amino acids. In the amino-terminal end of the coding sequence was a stretch of about 20 hydrophobic amino acids, but, in contrast to consensus signal peptides, no basic residues were present. The length of the second polypeptide was 227 amino acids. It was found that expression of the phospholipase gene in both E. coli and S. liquefaciens was growth phase regulated (late expression).
TidsskriftJournal of Bacteriology
Udgave nummer12
Sider (fra-til)5855-62
Antal sider8
StatusUdgivet - 1988
Eksternt udgivetJa

ID: 44293590