Nonsymbiotic hemoglobins and stress tolerance in plants.
Hemoglobins (Hbs) are heme containing proteins found in most organisms including animals, bacteria, and plants. Their structure, size, and function are quite diverse among the different organisms. There are three different types of hemoglobins in plants: symbiotic (sHb), nonsymbiotic (nsHb), and truncated hemoglobins (trHb). The nonsymbiotic hemoglobins are divided into: class 1 hemoglobins (nsHb-1s), which have a very high affinity for oxygen: and class 2 hemoglobins (nsHb-2s), which have lower affinity for oxygen, are similar to the sHbs. nsHb-1s are expressed under hypoxia, osmotic stress, nutrient deprivation, cold stress, rhizobial infection, nitric oxide exposure, and fungal infection. Tolerance to stress is very important for the survival of the plant. Hemoglobins are one of many different strategies that plants have evolved to overcome stress conditions and survive. Hbs also react with NO produced under different stress conditions. Class 1 nsHbs are involved in a metabolic pathway involving NO. Those hemoglobins provide an alternative type of respiration to mitochondrial electron transport under limiting oxygen concentrations. Class 1 nsHbs in hypoxic plants act as part of a soluble, terminal, NO dioxygenase system, yielding nitrate from the reaction of oxyHb with NO. The overall reaction sequence, referred to as the nsHb/NO cycle, consumes NADH and maintains ATP levels via an as yet unknown mechanism. Class 2 nsHbs seem to scavenge NO in a similar fashion as class 1 Hbs and are involved in reducing flowering time in Arabidopsis. nsHbs also show peroxidase-like activity and NO metabolism and possibly protect against nitrosative stress in plant-pathogen interaction and in symbiotic interactions. nsHbs may be involved in other stress conditions such as osmotic, nutrient and cold stress together with NO and the function of nsHbs can be in NO metabolism and signal transduction. However, other possible functions cannot be precluded as Hbs have many different functions in other organisms.
Aristotle University of Thessaloniki, Faculty of Agriculture, Laboratory of Agronomy, 54124 Thessaloniki, Greece. Electronic address: chdordas@agro.auth.gr.
Christos
C
Dordas
Hemoglobin; Hypoxia; Nitric oxide; Stress