Comprehensive egg-coat proteome of an ascidian
Ontology highlight
ABSTRACT:
INSTRUMENT(S): ESI-QUAD-TOF
ORGANISM(S): Ciona Intestinalis
SUBMITTER: 
Attila Csordas
LAB HEAD: Attila Csordas
PROVIDER: PRD000466 | Pride | 2012-07-26
REPOSITORIES: Pride
Dataset's files
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Project description:Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion.
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