Prohormone proteins in animals and yeast are typically processed at dibasic sites by convertases. Propeptide hormones are also found in plants but little is known about processing. We show for the first time that a dibasic site upstream of a plant peptide hormone, AtRALF1, is essential for processing. Overexpression of preproAtRALF1 causes semidwarfism whereas overexpression of preproAtRALF1(R69A), the propeptide with a mutation in the dibasic site, shows a normal phenotype. RALF1(R69A) plants accumulate only the mutated proprotein and not the processed peptide. In vitro processing using microsomal fractions suggests that processing is carried out by a kexin-like convertase.

The last century was the scene of an extraordinary social and economic development of mankind. This development had the fossil energy as one of its pillars. The discovery of petrol led the society to shape a development model highly dependent on this source of energy, which has finite resources and also promotes a big increase on the greenhouse gases, with unforeseeable consequences for the human beings as well as the entire life. It is imperative that we change the pillars of energy from fossil to renewables that will be more sustainable and less aggressive to the environment. One of the sources of this new energy platform, probably the best, is biomass. Fibrous plants bring several advantages and fit well within the requirements deemed important to be elected as producers of biomass. Among these characteristics we have the high processing capacity of solar energy into biomass, fast growth, long-term canopy, possibility of large-scale production. Despite of that this plants are adapted to suboptimal environments that allows its production not compete with food production because it requires less energy input, bringing marginal lands into production with its all social-benefit consequences. Among the fibrous plants, SUGAR CANE or, better, ENERGY CANE has one of the biggest potential for biomass productions. Results from several breeding programs has showing the high biomass potential of energy cane over other biomass crops like sorghum, elephant grass and eucalyptus.

rapid alkalinization factor 1 (AtRALF1) is a small secreted peptide hormone that inhibits root growth by repressing cell expansion. Although it is known that AtRALF1 binds the plasma membrane receptor FERONIA and conveys its signals via phosphorylation, the AtRALF1 signaling pathway is largely unknown. Here, using a yeast two-hybrid system to search for AtRALF1-interacting proteins in , we identified calmodulin-like protein 38 (CML38) as an AtRALF1-interacting partner. We also found that CML38 and AtRALF1 are both secreted proteins that physically interact in a Ca- and pH-dependent manner. CML38-knockout mutants generated via T-DNA insertion were insensitive to AtRALF1, and simultaneous treatment with both AtRALF1 and CML38 proteins restored sensitivity in these mutants. Hybrid plants lacking CML38 and having high accumulation of the AtRALF1 peptide did not exhibit the characteristic short-root phenotype caused by overexpression. Although CML38 was essential for AtRALF1-mediated root inhibition, it appeared not to have an effect on the AtRALF1-induced alkalinization response. Moreover, acridinium-labeling of AtRALF1 indicated that the binding of AtRALF1 to intact roots is CML38-dependent. In summary, we describe a new component of the AtRALF1 response pathway. The new component is a calmodulin-like protein that binds AtRALF1, is essential for root growth inhibition, and has no role in AtRALF1 alkalinization.