Abstract
The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel α-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 121-129 |
| Number of pages | 9 |
| Journal | Peptides |
| Volume | 26 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2005 |
Fingerprint
Keywords
- Albumen gland
- Aplysia
- Attractin
- Bursatella leachii
- Mollusk
- Protein pheromone
ASJC Scopus subject areas
- Biochemistry
- Endocrinology
- Physiology
- Cellular and Molecular Neuroscience
Cite this
Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness. / Cummins, Scott F.; Schein, Catherine H.; Xu, Yuan; Braun, Werner; Nagle, Gregg T.
In: Peptides, Vol. 26, No. 1, 01.2005, p. 121-129.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness
AU - Cummins, Scott F.
AU - Schein, Catherine H.
AU - Xu, Yuan
AU - Braun, Werner
AU - Nagle, Gregg T.
PY - 2005/1
Y1 - 2005/1
N2 - The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel α-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific.
AB - The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel α-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific.
KW - Albumen gland
KW - Aplysia
KW - Attractin
KW - Bursatella leachii
KW - Mollusk
KW - Protein pheromone
UR - http://www.scopus.com/inward/record.url?scp=11144314747&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=11144314747&partnerID=8YFLogxK
U2 - 10.1016/j.peptides.2004.07.017
DO - 10.1016/j.peptides.2004.07.017
M3 - Article
C2 - 15626512
AN - SCOPUS:11144314747
VL - 26
SP - 121
EP - 129
JO - Peptides
JF - Peptides
SN - 0196-9781
IS - 1
ER -