| Title: | Pherophorins: a family of extracellular matrix glycoproteins from Volvox structurally related to the sex-inducing pheromone |
| Author(s): | Godl K; Hallmann A; Rappel A; Sumper M; |
| Address: | "Lehrstuhl Biochemie I, Universitat Regensburg, Germany" |
| ISSN/ISBN: | 0032-0935 (Print) 0032-0935 (Linking) |
| Abstract: | "Pherophorins are extracellular matrix (ECM) glycoproteins from Volvox that share homology with the sex-inducing pheromone. A novel pherophorin (pherophorin III) was characterized both with respect to expression pattern and proteolytic processing in vivo. Furthermore, it was shown that the pherophorins represent a protein family of ECM glycoproteins exhibiting a modular composition: their N-terminally located domain is a homolog of a domain found in the ECM glycoprotein SSG 185. Together with SSG 185, pherophorin I is a main component of the cellular zone within the ECM. The Volvox genome contains a tandem arrangement of genes encoding pherophorin II-related polypeptides. Inhibition of proteolytic processing of pherophorin II and III in vivo appears to result in the suppression of sexual induction" |
| Keywords: | "Algal Proteins Amino Acid Sequence Chlorophyta/*chemistry/genetics/physiology Extracellular Matrix Proteins/*chemistry/genetics Glycoproteins/*chemistry/genetics Hydrolysis Molecular Sequence Data Multigene Family Sequence Homology, Amino Acid Sex Attract;" |
| Notes: | "MedlineGodl, K Hallmann, A Rappel, A Sumper, M eng Research Support, Non-U.S. Gov't Germany 1995/01/01 Planta. 1995; 196(4):781-7" |
