Differential targeting of closely related ECM glycoproteins: the pherophorin family from Volvox

• Published in: The EMBO journal Vol. 16; no. 1; pp. 25 - 34
• Main Authors: Godl, K, Hallmann, A, Wenzl, S, Sumper, M
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.01.1997
• Subjects: Algal Proteins; Amino Acid Sequence; amino acid sequences; arabinose; Arabinose - chemistry; arylsulfatase; Biological Transport; chemical structure; Chlorophycota; Chlorophyta; Chlorophyta - metabolism; Cloning, Molecular; complementary DNA; cytochemistry; ECM glycoproteins; extracellular matrix glycoproteins; Extracellular Matrix Proteins - chemistry; Extracellular Matrix Proteins - genetics; Extracellular Matrix Proteins - isolation & purification; Extracellular Matrix Proteins - metabolism; Freshwater; genbank/y07752; gene expression; glycoproteins; Glycoproteins - chemistry; Glycoproteins - genetics; Glycoproteins - isolation & purification; Glycoproteins - metabolism; green algae; hydroxyproline-rich glycoproteins; Molecular Sequence Data; molecular weight; nucleotide sequences; Peptides - chemistry; Pheromones - metabolism; pherophorins; Phosphoric Diester Hydrolases - chemistry; promoter regions; Promoter Regions, Genetic; recombinant DNA; reporter genes; Sequence Homology, Amino Acid; Transcription, Genetic; Volvox; Volvox carteri
• ISSN: 0261-4189; 1460-2075; 1460-2075
• DOI: 10.1093/emboj/16.1.25

The alga Volvox carteri represents one of the simplest multicellular organisms. Its extracellular matrix (ECM) is modified under developmental control, e.g. under the influence of the sex-inducing that triggers development of males and females at a concentration below 10(-6) M. A novel protein ECM glycoprotein (pherophorin-S) synthesized in response to this pheromone was identified and characterized. Although being a typical member of the pherophorins, which are identified by a C-terminal domain with homology to the sex-inducing pheromone, pherophorin-S exhibits a completely novel set of properties. In contrast to the other members of the family, which are found as part of the insoluble ECM structures of the cellular zone, pherophorin-S is targeted to the cell-free interior of the spherical organism and remains in a soluble state. A main structural difference is the presence of a polyhydroxyproline spacer in pherophorin-S that is linked to a saccharide containing a phosphodiester bridge between two arabinose residues. Sequence comparisons indicate that the self-assembling proteins that create the main parts of the complex Volvox ECM have evolved from a common ancestral gene.