| Title: | Transcriptional activation by the sexual pheromone and wounding: a new gene family from Volvox encoding modular proteins with (hydroxy)proline-rich and metalloproteinase homology domains |
| Author(s): | Hallmann A; Amon P; Godl K; Heitzer M; Sumper M; |
| Address: | "Lehrstuhl Biochemie I, Universitat Regensburg, Universitatstr. 31, D-93053 Regensburg, Germany. armin.hallmann@vkl.uni-regensburg.de" |
| DOI: | 10.1046/j.1365-313x.2001.01059.x |
| ISSN/ISBN: | 0960-7412 (Print) 0960-7412 (Linking) |
| Abstract: | "The green alga Volvox represents the simplest kind of multicellular organism: it is composed of only two cell types, somatic and reproductive, making it suitable as a model system. The sexual development of males and females of Volvox carteri is triggered by a sex-inducing pheromone at a concentration of < 10-16 M. Early biochemical responses to the pheromone involve structural modifications within the extracellular matrix (ECM). By differential screenings of cDNA libraries made from mRNAs of pheromone-treated Volvox, four novel genes were identified that encode four closely related Volvox metalloproteinases that we use to define a new protein family, the VMPs. The existence of several features common to matrix glycoproteins, such as signal peptides, a (hydroxy)proline content of 12-25%, and Ser(Pro)2-4 repeats, suggest an extracellular localization of the VMPs within the ECM. Synthesis of VMP cDNAs is triggered not only by the sex-inducing pheromone, but also by wounding, and is restricted to the somatic cell type. Sequence comparisons suggest that the VMPs are members of the MB clan of zinc-dependent matrix metalloproteinases, although the putative zinc binding site of all VMPs is QEXXHXXGXXH rather than HEXXHXXGXXH. The presence of glutamine instead of histidine in the zinc binding motif suggests a novel family, or even clan, of peptidases. Like the matrixin family of human collagenases, Volvox VMPs exhibit a modular structure: they possess a metalloproteinase homology domain and a (hydroxy)proline-rich domain, and one of them, VMP4, also has two additional domains. Metalloproteinases seem to be crucial for biochemical modifications of the ECM during development or after wounding in the lower eukaryote Volvox with only two cell types, just as in higher organisms" |
| Keywords: | "Amino Acid Sequence Base Sequence Chlorophyta/*genetics Cloning, Molecular DNA Primers DNA, Complementary Glycoproteins/chemistry/*genetics Metalloendopeptidases/chemistry/*genetics Molecular Sequence Data *Multigene Family *Plant Proteins RNA, Messenger/;" |
| Notes: | "MedlineHallmann, A Amon, P Godl, K Heitzer, M Sumper, M eng Research Support, Non-U.S. Gov't England 2001/08/08 Plant J. 2001 Jun; 26(6):583-93. doi: 10.1046/j.1365-313x.2001.01059.x" |
