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Fundulus heteroclitus vitellogenin: The deduced primary structure of a piscine precursor to noncrystalline,liquid-phase yolk protein
Authors:Gary J LaFleur Jr  B Marion Byrne  Jyotshnabala Kanungo  Laura D Nelson  Robert M Greenberg  Robin A Wallace
Institution:(1) Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd., 32086 Marineland, FL, USA;(2) Department of Anatomy and Cell Biology, College of Medicine, University of Florida, 32610 Gainesville, FL, USA;(3) Institute of Molecular Medicine and Genetics, Medical College of Georgia, 30912 Augusta, GA, USA
Abstract:We have cloned and sequenced a cDNA encoding a vitellogenin (Vtg) from the mummichog, Fundulus heteroclitus, an estuarine teleost. We constructed a liver cDNA library against RNA from estrogen-treated male mummichogs. Five overlapping cDNA clones totalling 5,197 by were isolated through a combination of degenerate oligonucleotide probing of the library and PCR. The cDNA sequence contains a 5,112 by open reading frame. The predicted primary structure of the deduced 1,704-amino-acid protein is 30–40% identical to other documented chordate Vtgs, establishing this Vtg as a member of the ancient Vtg gene family. Of the previously reported chordate Vtg sequences (Xenopus laevis, Gallus domesticus, Ichthyomyzon unicuspis, and Acipenser transmontanus), all four act as precursor proteins to a yolk which is eventually rendered insoluble under physiological conditions, either as crystalline platelets or as noncrystalline granules. The yolk of F. heteroclitus, on the other hand, remains in a soluble state throughout oocyte growth. The putative F. heteroclitus Vtg contains a polyserine region with a relative serine composition that is 10–20% higher than that observed for the other Vtgs. The trinucleotide repeats encoding the characteristic polyserine tracts of the phosvitin region follow a previously reported trend: TCX codons on the 5prime end and AGY codons toward the 3prime end. Whether the difference in Vtg primary structure between F. heteroclitus and that of other chordates is responsible for the differences in yolk structure remains to be elucidated. As the first complete teleost Vtg to be reported, these data will aid in designing nucleotide and immunological probes for detecting Vtg as a reproductive status indicator in F. heteroclitus and other piscine species.Abbreviations AGY AG(T or C) - TCX TC(AGC or T) - Lv lipovitellin - Pv phosvitin - Vtg vitellogenin Correspondence to: G.J. LaFleur, Jr.
Keywords:Vitellogenin  Vitellogenesis  Phosvitin  Lipovitellin  Yolk  Trinucleotide repeat  Teleost  Fundulus heteroclitus
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