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Journal of Experimental Biology, Vol 200, Issue 10 1483-1489, Copyright © 1997 by Company of Biologists

JOURNAL ARTICLES

Molecular analysis of FMRFamide- and FMRFamide-related peptides (FaRPS) in the cuttlefish Sepia officinalis

PK Loi and N Tublitz
Institute of Neuroscience, University of Oregon, Eugene 97403, USA. Loi@uoneuro.uoregon.edu

The display of complex color patterns of the cuttlefish Sepia officinalis is under the regulation of the FMRFamide-related peptide (FaRP) family, but their exact identities are unknown. We report the isolation and characterization of a full-length FaRP cDNA from the brain of S. officinalis. This cDNA is 1850 base pairs long, including an open reading frame of 996 base pairs. The cDNA encodes a precursor protein containing four FaRPs: ALSGDAFLRF, FIRF, FLRF and FMRF. Each propeptide has a C-terminal glycine residue that is presumably converted post-translationally to an amide. Every FaRP propeptide is also flanked by basic amino acid residues at the amino and carboxy termini, indicative of putative cleavage sites during post-translational processing. Each of the four FaRPs encoded by this cDNA causes chromatophore expansion when assayed in an in vitro chromatophore bioassay. Thus, it is likely that one or more of the FaRPs identified in this study are involved in controlling chromatophore activity in cuttlefish.


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© The Company of Biologists Ltd 1997