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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens. / Givskov, M; Olsen, L; Molin, Søren.

In: Journal of Bacteriology, Vol. 170, No. 12, 1988, p. 5855-62.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Givskov, M, Olsen, L & Molin, S 1988, 'Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens', Journal of Bacteriology, vol. 170, no. 12, pp. 5855-62.

APA

Givskov, M., Olsen, L., & Molin, S. (1988). Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens. Journal of Bacteriology, 170(12), 5855-62.

Vancouver

Givskov M, Olsen L, Molin S. Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens. Journal of Bacteriology. 1988;170(12):5855-62.

Author

Givskov, M ; Olsen, L ; Molin, Søren. / Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens. In: Journal of Bacteriology. 1988 ; Vol. 170, No. 12. pp. 5855-62.

Bibtex

@article{e50d33ad9dae4d5687f419c02c68c716,
title = "Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens",
abstract = "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).",
author = "M Givskov and L Olsen and S{\o}ren Molin",
year = "1988",
language = "English",
volume = "170",
pages = "5855--62",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "12",

}

RIS

TY - JOUR

T1 - Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciens

AU - Givskov, M

AU - Olsen, L

AU - Molin, Søren

PY - 1988

Y1 - 1988

N2 - 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).

AB - 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).

M3 - Journal article

C2 - 3056919

VL - 170

SP - 5855

EP - 5862

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 12

ER -

ID: 44293590