Adenylate cyclase (AC) (ATP diphosphate-lyase cyclizing; EC 4.6.1.1) is a key component of the adenylate cyclase signaling system and catalyzes the generation of cyclic adenosine monophosphate (cAMP) from ATP. This review summarizes data from the literature and the authors' laboratory on the investigation of plant transmembrane (tmAC) and soluble (sAC) adenylate cyclases, in comparison with some key characteristics of adenylate cyclases of animal cells. Plant sAC has been demonstrated to exhibit similarities with animal sAC with respect to certain characteristics. External factors, such as far-red and red light, temperature, exogenous phytohormones, as well as specific triggering compounds of fungal and bacterial origin exert a significant influence on the activity of plant tmAC and sAC.

Work was carried out on pea ( Pisum sativum L.) seedling roots to assess the attachment of the nitrogen-fixing symbiotic bacteria Rhizobium leguminosarum bv. vicea ( Rlv) and the bacterial...

Changes in hydrogen peroxide and cAMP concentrations in pea ( Pisum sativum L.) seedlings inoculated with Rhizobium leguminosarum bv. viceae Frank ( Rlv) were evaluated as related to a...

The possible role of transmembrane adenylate cyclase of a plant pathogen Pseudomonas siringae pv. pisi and of a symbiotroph Rhizobium leguminosarum bv. viceae in control of the activity of their virulence factors (cellulases and pectinases, the enzymes degrading plant cell walls) was investigated. While transmembrane adenylate cyclase was found to control the activity of virulence factors in both pathogens and symbionts, the strategies employed by these microorganisms in molecular dialogue with plants involving the adenylate cylcase signal system exhibited both similarities and cardinal differences.

The effect of N-phenyl-2-naphthylamine, negative allelochemical isolated from the exudates of roots of pea (Pisum sativum L.), on the growth and activity of the adenylate cyclase signal system and virulence factors of the bacteria Rhizobium leguminosarum bv. viciae and Pseudomonas siringae pv. pisi was studied. It was demonstrated that N-phenyl-2-naphthylamine at a physiological concentration nonspecifically inhibited the growth of these bacteria in both planktonic cultures and biofilms. One of the reasons for this phenomenon is the reduction of intra- and extracellular concentrations of cAMP due to greater activation of phosphodiesterase, which disrupts cAMP, in comparison to soluble adenylyl cyclase, which synthesizes it. At the same time, N-phenyl-2-naphthylamine did not affect activity of either membrane-bound adenylyl cyclase or bacterial virulence factors.