Joelle Marechal

A possible role for phenyl acetic acid (PAA) on Alnus glutinosa nodulation by Frankia

Phenylacetic hopanetetrol is a Frankia specific lipid present in vesicles. Phenylacetic acid (PAA) is known as an auxinomimetic, exhibiting the same effect on plant growth as indole acetic acid (IAA). We hypothesize that PAA, only bound by an ester link to the hopanetetrol basic unit, would be easily released and could thus play a role in nodule formation. HPLC and mass spectrometry analysis allowed us to show that 2 Alnus- (ACoN24d and ACN14a) and 2 Elaeagnus-infective strains (EaI1 and EaI3) released PAA into the culture medium, at concentrations of about 10−5 to 10−6 M, whereas IAA was not detected. Furthermore, exogenous PAA added to axenically-grown Alnus glutinosa roots at a concentration of 5 × 10−5 M, resulted in the formation of thick, short lateral roots which resembled actinorhizal nodules. phenylalanine ammonia lyase (PAL) and chalcone syntase (CHS) induction by incompatible and compatible Frankia strains in A. glutinosa roots and the different contents in salicylic acid precursors (cinnamic acid and benzoic acid) observed between nodules and roots support the idea that PAA would be produced in nodules to the detriment of salicylic acid production. These results provide evidence that in actinorhizal root nodules, phenylpropanoid metabolism may play a multiple role in symbiotic interactions including the limitation of the induction of the systematic acquired resistance (SAR) by the plant.

Lectin genes in the Frankia alni genome

Frankia alni strain ACN14a’s genome was scanned for the presence of determinants involved in interactions with its host plant, Alnus spp. One such determinant type is lectin, proteins that bind specifically to sugar motifs. The genome of F. alni was found to contain 7 such lectin-coding genes, five of which were of the ricinB-type. The proteins coded by these genes contain either only the lectin domain, or also a heat shock protein or a serine-threonine kinase domain upstream. These lectins were found to have several homologs in Streptomyces spp., and a few in other bacterial genomes among which none in Frankia EAN1pec and CcI3 and two in strain EUN1f. One of these F. alni genes, FRAAL0616, was cloned in E. coli, fused with a reporter gene yielding a fusion protein that was found to bind to both root hairs and to bacterial hyphae. This protein was also found to modify the dynamics of nodule formation in A. glutinosa, resulting in a higher number of nodules per root. Its role could thus be to permit binding of microbial cells to root hairs and help symbiosis to occur under conditions of low Frankia cell counts such as in pioneer situations.