Structural and functional analysis of Aplysia attractins, a family of water-borne protein pheromones with interspecific attractiveness.

Abstract:

:Mate attraction in Aplysia involves a long-distance water-borne signal (the protein pheromone attractin), which is released during egg laying. Aplysia californica attractin attracts species that produce closely related attractins, such as Aplysia brasiliana, whose geographic distribution does not overlap that of A. californica. This finding suggests that other mollusks release attractin-related pheromones to form and maintain breeding aggregations. We describe four additional members of the attractin family: A. brasiliana, Aplysia fasciata, Aplysia depilans (which aggregates with A. fasciata aggregations), and Aplysia vaccaria (which aggregates with A. californica aggregations). On the basis of their sequence similarity with A. californica attractin, the attractin proteins fall into two groups: A. californica, A. brasiliana, and A. fasciata (91-95% identity), and A. depilans and A. vaccaria (41-43% identity). The sequence similarity within the attractin family, the conserved six cysteines, and the compact fold of the NMR solution structure of A. californica attractin suggest a common fold for this pheromone family containing two antiparallel helices. The second helix contains the IEECKTS sequence conserved in Aplysia attractins. Mutating surface-exposed charged residues within this heptapeptide sequence abolishes attractin activity, suggesting that the second helix is an essential part of the receptor-binding interface.

authors

Painter SD,Cummins SF,Nichols AE,Akalal DB,Schein CH,Braun W,Smith JS,Susswein AJ,Levy M,de Boer PA,ter Maat A,Miller MW,Scanlan C,Milberg RM,Sweedler JV,Nagle GT

doi

10.1073/pnas.0306339101

keywords:

subject

Has Abstract

pub_date

2004-05-04 00:00:00

pages

6929-33

issue

18

eissn

0027-8424

issn

1091-6490

pii

0306339101

journal_volume

101

pub_type

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