Molecular characterization of a gene encoding the Drosophila melanogaster phospholipase A2.
A gene encoding Drosophila melanogaster secretory phospholipase A2 (sPLA2) has been cloned and characterized(.) The coding region of the sPLA2 gene was interrupted by a short intron, and codes for a signal peptide of 18 amino acids, followed by a mature protein of 168 amino acids, containing the structural features of group III sPLA2. From a Northern blot analysis, about a 1.0-kb Drosophila sPLA2 transcript was found to be expressed throughout its development and in both the adult bodies and heads. The recombinant Drosophila sPLA2 expressed and purified in Escherichia coli was found to be Ca(+2)-dependent and maximally active at pH 5.
Ryu
Yoonseok
Y
Institute of Life Sciences and Resources, and Graduate School of Biotechnology, Kyung Hee University, Yongin 449-701, South Korea.
Oh
Younsang
Y
Yoon
Jaeseung
J
Cho
Wonhwa
W
Baek
Kwanghee
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D007814:Larva / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000235:genetics*; D054467:Phospholipases A2; D011679:Pupa / Q000201:enzymology / Q000235:genetics; D017422:Sequence Analysis, DNA
D010741:Phospholipases A; D054467:Phospholipases A2