Aplysia temptin - the ' glue ' in the water-borne attractin pheromone complex

Cummins, Scott F., Xie, Fang, de Vries, Melissa R., Annangudi, Suresh P., Misra, Milind, Degnan, Bernard M., Sweedler, Jonathan V., Nagle, Gregg T. and Schein, Catherine H. (2007) Aplysia temptin - the ' glue ' in the water-borne attractin pheromone complex. The FEBS Journal, 274 20: 5425-5437.


Author Cummins, Scott F.
Xie, Fang
de Vries, Melissa R.
Annangudi, Suresh P.
Misra, Milind
Degnan, Bernard M.
Sweedler, Jonathan V.
Nagle, Gregg T.
Schein, Catherine H.
Title Aplysia temptin - the ' glue ' in the water-borne attractin pheromone complex
Formatted title Aplysia temptin - the ' glue ' in the water-borne attractin pheromone complex
Journal name The FEBS Journal   Check publisher's open access policy
ISSN 1742-464X
1742-4658
Publication date 2007-10
Sub-type Article (original research)
DOI 10.1111/j.1742-4658.2007.06070.x
Volume 274
Issue 20
Start page 5425
End page 5437
Total pages 13
Editor R. Perham
Place of publication Oxford, England
Publisher Blackwell Publishing
Collection year 2008
Language eng
Subject C1
270702 Marine and Estuarine Ecology (incl. Marine Ichthyology)
770302 Living resources (incl. impacts of fishing on non-target species)
Abstract Temptin, a component of the complex of water-borne protein pheromones that stimulate attraction and mating behavior in the marine mollusk Aplysia, has sequence homology to the epidermal growth factor (EGF)-like domains of higher organisms that mediate protein-cell surface contact during fertilization and blood coagulation. In this work, recombinant temptin for structural and functional studies was produced in Escherichia coli using a cold shock promoter and purified by RP-HPLC. CD spectra confirmed a predominantly beta-sheet structure. Two disulfide bonds were determined via limited proteolysis and MS. One internal disulfide (Cys57-Cys77) was predicted from initial alignments with class I EGF-like domains; the second, between Cys18 and Cys103, could protect temptin against proteolysis in seawater and stabilize its interacting surface. A three-dimensional model of temptin was prepared with our MPACK suite, based on the Ca2+-binding, EGF-like domain of the extracellular matrix protein fibrillin. Two temptin residues, Trp52 and Trp79, which align with cysteine residues conserved in fibrillins, lie adjacent to and could stabilize the disulfide bonds and a proposed metal-binding loop. The water-borne pheromone attractin in egg cordon eluates is complexed with other proteins. Docking results with our model and the NMR structure of attractin suggest that one face of temptin interacts with the pheromone, perhaps controlling its access to the cellular receptors. Gel shifts confirmed that temptin complexes with wild-type attractin. These results indicate that temptin, analogous to the role of fibrillin in controlling transforming growth factor-beta concentration, modulates pheromone signaling by direct binding to attractin.
Keyword Biochemistry & Molecular Biology
enticin
fibrillin
epidermal growth factor-like domains
Marfan's syndrome
signaling network
Epidermal-growth-factor
Circular-dichroism Spectra
Protein Secondary Structure
Stimulate Mate Attraction
Factor-like Domains
Interspecific Attractiveness
Peptide Pheromone
Marfan-syndrome
Mutations
Disorders
Q-Index Code C1
Q-Index Status Confirmed Code

 
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Created: Mon, 18 Feb 2008, 15:15:55 EST