« Previous AbstractA Review about the Recent Advances in Selected NonThermal Plasma Assisted Solid-Gas Phase Chemical Processes    Next Abstract"Rapid evolution of plethodontid modulating factor, a hypervariable salamander courtship pheromone, is driven by positive selection" »

FEBS J

Title:		"Plethodontid modulating factor, a hypervariable salamander courtship pheromone in the three-finger protein superfamily"
Author(s):		Palmer CA; Hollis DM; Watts RA; Houck LD; McCall MA; Gregg RG; Feldhoff PW; Feldhoff RC; Arnold SJ;
Address:		"Department of Zoology, Oregon State University, Corvallis, OR 97331-2914, USA. cpalmer@pdx.edu"
Journal Title:		FEBS J
Year:		2007
Volume:		20070405
Issue:		9
Page Number:		2300 - 2310
DOI:		10.1111/j.1742-4658.2007.05766.x
ISSN/ISBN:		1742-464X (Print) 1742-464X (Linking)
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"
Keywords:		"Amino Acid Sequence Amphibian Proteins/biosynthesis/*chemistry/genetics/physiology Animals Conserved Sequence *Courtship Evolution, Molecular Female Genetic Variation Humans Male Molecular Sequence Data *Multigene Family Organ Specificity/genetics Protein;"
Notes:		"MedlinePalmer, Catherine A Hollis, David M Watts, Richard A Houck, Lynne D McCall, Maureen A Gregg, Ronald G Feldhoff, Pamela W Feldhoff, Richard C Arnold, Stevan J eng Comparative Study Research Support, U.S. Gov't, Non-P.H.S. England 2007/04/11 FEBS J. 2007 May; 274(9):2300-10. doi: 10.1111/j.1742-4658.2007.05766.x. Epub 2007 Apr 5"