title: Adaptive dynamics with a single two-state protein.
abstract: An important step towards understanding biological systems is to relate simple biochemical elements to dynamics. Here, we present the arguably simplest dynamical element in biochemical networks. It consists of a single protein with two states (active and inactive) and an external signal that catalyses the conversion between these two states. Further, there is steady synthesis and degradation of the inactive and active forms, respectively. As this element captures both structural and dynamical features of biochemical networks at the lowest level, we refer to it as a biochemical network unit (BioNetUnit). Using both simulations and mathematical analysis, we find that BioNetUnit shows perfect adaptation that leads to temporal responses to step changes in the incoming signal. Compared with a well-described adaptive system, which is found in bacterial chemotaxis, BioNetUnit has lower sensitivity and its adaptation time is less robust to the base signal levels. We show that these dynamical limitations lead to 'once-and-only-once' responses for certain signal sequences. These findings demonstrate that BioNetUnit is relevant in adaptive and cyclic processes. In particular, it could be seen as a generic representation for ligand-activated receptors that are desensitized upon continuous activation. The analysis of coupled BioNetUnits will show how the presented dynamics at single unit will change upon increased system complexity and how such systems would mediate biological functions.
authors.affiliation: Microsoft Research-University of Trento Centre for Computational and Systems Biology, Piazza Manci 17, Povo (Trento), Italy. csikasz@cosbi.eu
authors.forename: Attila
authors.initials: A
authors.lastname: Csikász-Nagy
authors.forename: Orkun S
authors.initials: OS
authors.lastname: Soyer
mesh_terms: D000222:Adaptation, Physiological; D018407:Bacterial Physiological Phenomena; D002633:Chemotaxis; D008024:Ligands; D008954:Models, Biological; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D008024:Ligands; D011506:Proteins; D011956:Receptors, Cell Surface