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Relationships among the FMRFamide-like peptides.

M J Greenberg1, D A Price

  • 1Whitney Laboratory, University of Florida, St. Augustine 32086-8623.

Progress in Brain Research
|January 1, 1992
PubMed
Summary

The nuclear family of peptides, FaRPs (FMRFamide-related peptides), is found in protostome invertebrates. The broader superfamily of FaRPs, however, is present across all animal phyla, suggesting ancient origins and diverse functions.

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Invertebrate Zoology

Background:

  • The FMRFamide-related peptides (FaRPs) nuclear family is primarily identified in protostome invertebrates like mollusks, arthropods, annelids, and nematodes.
  • The evolutionary origins and full taxonomic range of the FaRPs family remain incompletely understood, with homologs not yet confirmed in flatworms and related phyla largely unexamined.

Purpose of the Study:

  • To investigate the distribution and evolutionary history of the FMRFamide-related peptides (FaRPs) family across diverse animal phyla.
  • To explore the potential functional significance of the conserved penultimate Arginine residue in FaRPs.

Main Methods:

  • Comparative sequence analysis of peptides across various invertebrate and vertebrate phyla.
  • Review of existing literature on FMRFamide-related peptides (FaRPs) and their homologs.
  • Phylogenetic analysis to infer evolutionary relationships of FaRPs.

Main Results:

  • The nuclear FaRPs family appears restricted to protostome invertebrates.
  • An extended superfamily of FaRPs, characterized by a penultimate Arg and a C-terminal amidated hydrophobic residue, is found in all examined phyla.
  • The penultimate Arginine residue may confer protection against deamidating peptidases.

Conclusions:

  • The broad distribution of the extended FaRPs superfamily suggests an ancient origin and conserved biological roles.
  • The restricted distribution of the nuclear FaRPs family highlights evolutionary divergence within this peptide group.
  • Conserved receptor binding or protection against enzymatic degradation are potential selective advantages for FaRPs.

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