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

Sherry D. Painter, Scott F. Cummins, Amy E. Nichols, David B.G. Akalal, Catherine H. Schein, Werner Braun, John S. Smith, Abraham J. Susswein, Miriam Levy, Pamela A.C.M. De Boer, Andries Ter Maat, Mark W. Miller, Cory Scanlan, Richard M. Milberg, Jonathan V. Sweedler, Gregg Thomas Nagle

Research output: Contribution to journalArticle

46 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)6929-6933
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number18
DOIs
StatePublished - May 4 2004
Externally publishedYes

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Aplysia
Pheromones
Water
Vaccaria
Proteins
Conserved Sequence
Mollusca
Breeding
Ovum
Cysteine

ASJC Scopus subject areas

  • General

Cite this

Structural and functional analysis of Aplysia attractins, a family of water-borne protein pheromones with interspecific attractiveness. / Painter, Sherry D.; Cummins, Scott F.; Nichols, Amy E.; Akalal, David B.G.; Schein, Catherine H.; Braun, Werner; Smith, John S.; Susswein, Abraham J.; Levy, Miriam; De Boer, Pamela A.C.M.; Ter Maat, Andries; Miller, Mark W.; Scanlan, Cory; Milberg, Richard M.; Sweedler, Jonathan V.; Nagle, Gregg Thomas.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, No. 18, 04.05.2004, p. 6929-6933.

Research output: Contribution to journalArticle

Painter, SD, Cummins, SF, Nichols, AE, Akalal, DBG, Schein, CH, Braun, W, Smith, JS, Susswein, AJ, Levy, M, De Boer, PACM, Ter Maat, A, Miller, MW, Scanlan, C, Milberg, RM, Sweedler, JV & Nagle, GT 2004, 'Structural and functional analysis of Aplysia attractins, a family of water-borne protein pheromones with interspecific attractiveness', Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 18, pp. 6929-6933. https://doi.org/10.1073/pnas.0306339101
Painter, Sherry D. ; Cummins, Scott F. ; Nichols, Amy E. ; Akalal, David B.G. ; Schein, Catherine H. ; Braun, Werner ; Smith, John S. ; Susswein, Abraham J. ; Levy, Miriam ; De Boer, Pamela A.C.M. ; Ter Maat, Andries ; Miller, Mark W. ; Scanlan, Cory ; Milberg, Richard M. ; Sweedler, Jonathan V. ; Nagle, Gregg Thomas. / Structural and functional analysis of Aplysia attractins, a family of water-borne protein pheromones with interspecific attractiveness. In: Proceedings of the National Academy of Sciences of the United States of America. 2004 ; Vol. 101, No. 18. pp. 6929-6933.
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AU - Painter, Sherry D.

AU - Cummins, Scott F.

AU - Nichols, Amy E.

AU - Akalal, David B.G.

AU - Schein, Catherine H.

AU - Braun, Werner

AU - Smith, John S.

AU - Susswein, Abraham J.

AU - Levy, Miriam

AU - De Boer, Pamela A.C.M.

AU - Ter Maat, Andries

AU - Miller, Mark W.

AU - Scanlan, Cory

AU - Milberg, Richard M.

AU - Sweedler, Jonathan V.

AU - Nagle, Gregg Thomas

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N2 - 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.

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