Proteases hold the key to an exclusive mutualism.
Mutualisms, cooperative interactions between species, generally involve an economic exchange: species exchange commodities that are cheap for them to provide, for ones that cannot be obtained affordably or at all. But these associations can only succeed if effective partners can be enticed to interact. In some mutualisms, partners can actively seek one another out. However, plants, which use mutualists for a wide array of essential life history functions, do not have this option. Instead, natural selection has repeatedly favoured the evolution of rewards – nutritional substances (such as sugar-rich nectar and fleshy fruit) with which plants attract certain organisms whose feeding activities can then be co-opted for their own benefit. The trouble with rewards, however, is that they are usually also attractive to organisms that confer no benefits at all. Losing rewards to 'exploiters' makes a plant immediately less attractive to the mutualists it requires; if the reward cannot be renewed quickly (or at all), then mutualistic service is precluded entirely. Thus, it is in plants' interests to either restrict rewards to only the most beneficial partners or somehow punish or deter exploiters. Yet, at least in cases where the rewards are highly nutritious, we can expect counter-selection for exploiter traits that permit them to skirt such control. How, then, can mutualisms persist? In this issue, Orona-Tamayo et al. () describe a remarkable adaptation that safeguards one particularly costly reward from nonmutualists. Their study helps to explain the evolutionary success of an iconic interaction and illuminates one way in which mutualism as a whole can persist in the face of exploitation.
Department of Ecology and Evolutionary Biology, University of Arizona, Tucson, AZ 85745, USA. judieb@email.arizona.edu
Judith L
JL
Bronstein
D000045:Acacia / Q000201:enzymology*; D000818:Animals; D001000:Ants / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism*; D013559:Symbiosis / Q000502:physiology*
D011480:Protease Inhibitors; D010447:Peptide Hydrolases