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
A. Hallmann et al., 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, PLANT J, 26(6), 2001, pp. 583-593
The green alga Volvox represents the simplest kind of multicellular organis
m: 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 concentrati
on of < 10(-16) M. Early biochemical responses to the pheromone involve str
uctural modifications within the extracellular matrix (ECM). By differentia
l screenings of cDNA libraries made from mRNAs of pheromone-treated Volvox,
four novel genes were identified that encode four closely related Volvox m
etalloproteinases that we use to define a new protein family, the VMPs. The
existence of several features common to matrix glycoproteins, such as sign
al peptides, a (hydroxy)proline content of 12-25%, and Ser(Pro)(2-4) repeat
s, suggest an extracellular localization of the VMPs within the ECM. Synthe
sis of VMP cDNAs is triggered not only by the sex-inducing pheromone, but a
lso by wounding, and is restricted to the somatic cell type. Sequence compa
risons suggest that the VMPs are members of the MB clan of zinc-dependent m
atrix metalloproteinases, although the putative zinc binding site of all VM
Ps is QEXXHXXGXXH rather than HEXXHXXGXXH. The presence of glutamine instea
d of histidine in the zinc binding motif suggests a novel family, or even c
lan, 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 biochemi
cal modifications of the ECM during development or after wounding in the lo
wer eukaryote Volvox with only two cell types, just as in higher organisms.