How a sex pheromone might act at a concentration below 10(-16) M

• Published in: The EMBO journal Vol. 12; no. 3; pp. 831 - 836
• Main Authors: Sumper, M, Berg, E, Wenzl, S, Godl, K
• Format: Journal Article
• Language: English
• Published: England 01.03.1993
• Subjects: Algal Proteins; Amino Acid Sequence; amino acid sequences; Animals; Base Sequence; cell differentiation; Chlorophycota; Chlorophyta; complementary DNA; DNA; Extracellular Matrix Proteins - biosynthesis; Extracellular Matrix Proteins - genetics; Extracellular Matrix Proteins - isolation & purification; Extracellular Matrix Proteins - metabolism; Extracellular Matrix Proteins - pharmacology; Female; genbank/x69801; genbank/x69802; gene expression; genetic regulation; glycoproteins; Glycoproteins - biosynthesis; Glycoproteins - genetics; Glycoproteins - isolation & purification; Glycoproteins - metabolism; Glycoproteins - pharmacology; Male; Molecular Sequence Data; nucleotide sequences; pherophorin i; pherophorin ii; Polymerase Chain Reaction; proteolysis; Sequence Homology, Amino Acid; Sex Attractants - biosynthesis; Sex Attractants - genetics; Sex Attractants - isolation & purification; Sex Attractants - pharmacology; sex pheromones; sexual development; transcription (genetics); Transcription, Genetic; volvox carteri
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1993.tb05723.x

The sex-inducing pheromone of Volvox catteri is a glycoprotein that triggers development of males and females at a concentration below 10(-16) M. Evidence is presented for the existence of a novel mechanism of signal amplification operating within the extracellular matrix of this multicellular organism. A family of 70 kDa matrix glycoproteins denoted pherophorins bear a C-terminal domain being homologous to the sex-inducing pheromone. Under the influence of the pheromone, this domain is liberated by highly specific proteolysis.