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BOR - Papers in Press, published online ahead of print February 21, 2007.
Biol Reprod 2007, 10.1095/biolreprod.106.055772
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Submitted July 18, 2006
Returned for revision August 24, 2006
Accepted February 20, 2007

Gamete Biology


The Maturational Disassembly and Differential Proteolysis of Paralogous Vitellogenins in a Marine Pelagophil Teleost: A Conserved Mechanism of Oocyte Hydration

Roderick Nigel Finn *

* To whom correspondence should be addressed. E-mail: nigel.finn{at}bio.uib.no.

Abstract
A structural analysis of the differential proteolysis of vitellogenin (Vtg)-derived yolk proteins in the maturing oocytes of a marine teleost that spawns very large pelagic eggs is presented. Two full-length hepatic cDNAs encoding paralogous vitellogenins (cDNAs: hhvtgAa and hhvtgAb; encoding proteins: HhvtgAa and HhvtgAb) were cloned from non-estrogenized Atlantic halibut and the N-termini of their sub-domain structures mapped to the oocyte and egg yolk proteins (Yp). The maturational oocyte Yp degradation products were further mapped to the free amino acid (FAA) pool in the ovulated egg. Deduced amino acid sequences conformed to the linear NH2-(LvH-Pv-LvL-beta'-CT)-COO- structure for complete teleost Vtgs. However, the Yps did not match the expected cleavage products of complete Vtgs. Specifically, the phosvitin sub-domain of the HhvtgAa paralogue remains covalently attached to the lipovitellin light chain, while the phosvitin sub-domain of the HhvtgAb paralogue remains covalently attached to a C-terminal fragment of the lipovitellin heavy chain (LvH). During oocyte hydration, the LvH of the HhvtgAa paralogue is disassembled and extensively degraded to FAA. In the HhvtgAb paralogue, the LvH is nicked in the C-sheet in a manner similar to lamprey and other teleosts. A small part of the C-teminal end of the LvH-Ab is proteolysed to FAA, together with the phosvitin, beta'-component, and much (~65%) of the lipovitellin light chain (LvL-Ab). The independently measured FAA pool in the ovulated egg corroborates that calculated from the differential proteolysis of the Yps. Due to the 3:1 (HhvtgAb:HhvtgAa) Yp expression ratio, each paralogue contributes approximately equal amounts of FAA to the organic osmolyte pool of the hydrating oocyte during maturation.

Key words: Gamete Biology • Gametogenesis • Meiosis • Oocyte development • Ovulation





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