Open AccessExpression cloning of a cDNA encoding a fish prolactin receptor.
Author(s) -
Olivier Sandra,
Frédéric Sohm,
Amaury de Luze,
Patrick Prunet,
Marc Edery,
P. A. Kelly
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.13.6037
Subject(s) - biology , complementary dna , prolactin receptor , amino acid , microbiology and biotechnology , prolactin , peptide sequence , expression cloning , cdna library , receptor , cloning (programming) , northern blot , molecular cloning , biochemistry , gene , hormone , computer science , programming language
By using an expression cloning strategy, we isolated a single positive clone encoding a tilapia prolactin (PRL) receptor. Tilapia PRL188 was used to screen a freshwater tilapia kidney expression library transfected in COS cells. The tilapia PRL receptor is a mature protein of 606 amino acids. The extracellular domain is devoid of the tandem repeat units present in birds and has two pairs of cysteine residues, a Trp-Ser-Xaa-Trp-Ser motif, and two potential N-glycosylation sites. The cytoplasmic domain contains 372 amino acids, including box 1, a sequence previously shown to be important for signal transduction in mammalian species. Thus, the general structure is similar to the long form of mammalian PRL receptors; however, amino acid comparisons reveal a rather low identity (approximately 37%). Northern blot analysis shows the existence of a single transcript in osmoregulatory tissues and reproductive organs. This localization is in agreement with known functions of PRL in teleosts.