title: Plethodontid modulating factor, a hypervariable salamander courtship pheromone in the three-finger protein superfamily.
abstract: The soluble members of the three-finger protein superfamily all share a relatively simple 'three-finger' structure, yet perform radically different functions. Plethodontid modulating factor (PMF), a pheromone protein produced by the lungless salamander, Plethodon shermani, is a new and unusual member of this group. It affects female receptivity when delivered to the female's nares during courtship. As with other plethodontid pheromone genes, PMF is hyperexpressed in a specialized male mental (chin) gland. Unlike other plethodontid pheromone genes, however, PMF is also expressed at low levels in the skin, liver, intestine and kidneys of both sexes. The PMF sequences obtained from all tissue types were highly variable, with 103 unique haplotypes identified which averaged 35% sequence dissimilarity (range 1-60%) at the protein level. Despite this variation, however, all PMF sequences contained a conserved approximately 20-amino-acid secretion signal sequence and a pattern of eight cysteines that is also found in cytotoxins and short neurotoxins from snake venoms, as well as xenoxins from Xenopus. Although they share a common cysteine pattern, PMF isoforms differ from other three-finger proteins in: (a) amino-acid composition outside of the conserved motif; (b) length of the three distinguishing 'fingers'; (c) net charge at neutral pH. Whereas most three-finger proteins have a net positive charge at pH 7.0, PMF has a high net negative charge at neutral pH (pI range of most PMFs 3.5-4.0). Sequence comparisons suggest that PMF belongs to a distinct multigene subfamily within the three-finger protein superfamily.
authors.affiliation: Department of Zoology, Oregon State University, Corvallis, OR 97331-2914, USA. cpalmer@pdx.edu
authors.forename: Catherine A
authors.initials: CA
authors.lastname: Palmer
authors.forename: David M
authors.initials: DM
authors.lastname: Hollis
authors.forename: Richard A
authors.initials: RA
authors.lastname: Watts
authors.forename: Lynne D
authors.initials: LD
authors.lastname: Houck
authors.forename: Maureen A
authors.initials: MA
authors.lastname: McCall
authors.forename: Ronald G
authors.initials: RG
authors.lastname: Gregg
authors.forename: Pamela W
authors.initials: PW
authors.lastname: Feldhoff
authors.forename: Richard C
authors.initials: RC
authors.lastname: Feldhoff
authors.forename: Stevan J
authors.initials: SJ
authors.lastname: Arnold
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D000818:Animals; D017124:Conserved Sequence; D003380:Courtship; D019143:Evolution, Molecular; D005260:Female; D014644:Genetic Variation; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D005810:Multigene Family; D009928:Organ Specificity / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000502:physiology; D012724:Sex Attractants / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D014562:Caudata / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
chemical_list: D029845:Amphibian Proteins; C121545:PRF protein, Plethodon jordani; D012724:Sex Attractants