This paper originates from an address at the 8th International Symposium on Nitrogen Fixation with Non-Legumes, Sydney, NSW, December 2000 Azospirilla are free-living rhizobacteria that are able to promote plant growth and increase yields in many crops of agronomic importance. It is assumed that the bacteria affect plant growth mainly by the production of plant growth promoting substances, which leads to an improvement in root development and an increase in the rate of water and mineral uptake. In the present review, we discuss the physiological responses of the plant roots to inoculation with Azospirillum, and report on field and greenhouse experiments carried out with these bacteria during 1994–2001 in Belgium, Uruguay, Mexico and Israel.

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The CelA ␤-glucosidase of Azospirillum irakense, belonging to glycosyl hydrolase family 3 (GHF3), preferentially hydrolyzes cellobiose and releases glucose units from the C 3 , C 4 , and C 5 oligosaccharides. The growth of a ⌬celA mutant on these cellobiosides was affected. In A. irakense, the GHF3 ␤-glucosidases appear to be functional alternatives for the GHF1 ␤-glucosidases in the assimilation of ␤-glucosides by other bacteria.

The salAB genes of Azospirillum irakense KBC1, which encode two aryl-beta-glucosidases, are required for growth on salicin. In the 4-kb region upstream of the salAB genes, two additional genes, salC and salR, were identified. SalC shows characteristics of the outer membrane receptors in the FepA/FhuA family. The salC AB genes are transcribed as a polycistronic mRNA. The salR gene encodes a protein homologous to the LacI/GalR family of transcriptional repressors. Expression of the sal operon, measured by means of a salC-gusA translational fusion in A. irkense KBC1, requires the presence of aryl-beta-glucosides such as arbutin and salicin. Expression is markedly enhanced when a simple carbon source, like glucose, cellobiose or malate, is added to the medium. In a salR mutant, expression of the salC-gusA fusion does not require an aryl-beta-glucoside inducer. Expression of a salR-gusA fusion is constitutive. The product of arbutin hydrolysis (hydroquinone) partly inhibits the expression of a salC-gusA fusion in arbutin- or salicin-containing minimal medium. This effect is independent of SalR. Salicylalcohol, the hydrolysis product of salicin, also partly inhibits salC expression in a SalR-independent fashion, but only in salicin-containing minimal medium.