| Title: | Differential targeting of closely related ECM glycoproteins: the pherophorin family from Volvox |
| Author(s): | Godl K; Hallmann A; Wenzl S; Sumper M; |
| Address: | "Lehrstuhl Biochemie I, Universitat Regensburg, Germany" |
| ISSN/ISBN: | 0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking) |
| Abstract: | "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 pheromone that triggers development of males and females at a concentration below 10(-16) M. A novel 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 sequence 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" |
| Keywords: | "Algal Proteins Amino Acid Sequence Arabinose/chemistry Biological Transport Chlorophyta/*metabolism Cloning, Molecular Extracellular Matrix Proteins/chemistry/genetics/isolation & purification/*metabolism Glycoproteins/chemistry/genetics/isolation & purif;" |
| Notes: | "MedlineGodl, K Hallmann, A Wenzl, S Sumper, M eng Research Support, Non-U.S. Gov't England 1997/01/02 EMBO J. 1997 Jan 2; 16(1):25-34. doi: 10.1093/emboj/16.1.25" |
