title: Ethylene Regulates the Physiology of the Cyanobacterium Synechocystis sp. PCC 6803 via an Ethylene Receptor.
abstract: Ethylene is a plant hormone that plays a crucial role in the growth and development of plants. The ethylene receptors in plants are well studied, and it is generally assumed that they are found only in plants. In a search of sequenced genomes, we found that many bacterial species contain putative ethylene receptors. Plants acquired many proteins from cyanobacteria as a result of the endosymbiotic event that led to chloroplasts. We provide data that the cyanobacterium Synechocystis (Synechocystis sp. PCC 6803) has a functional receptor for ethylene, Synechocystis Ethylene Response1 (SynEtr1). We first show that SynEtr1 directly binds ethylene. Second, we demonstrate that application of ethylene to Synechocystis cells or disruption of the SynEtr1 gene affects several processes, including phototaxis, type IV pilus biosynthesis, photosystem II levels, biofilm formation, and spontaneous cell sedimentation. Our data suggest a model where SynEtr1 inhibits downstream signaling and ethylene inhibits SynEtr1. This is similar to the inverse-agonist model of ethylene receptor signaling proposed for plants and suggests a conservation of structure and function that possibly originated over 1 billion years ago. Prior research showed that SynEtr1 also contains a light-responsive phytochrome-like domain. Thus, SynEtr1 is a bifunctional receptor that mediates responses to both light and ethylene. To our knowledge, this is the first demonstration of a functional ethylene receptor in a nonplant species and suggests that that the perception of ethylene is more widespread than previously thought.
authors.affiliation: Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840.
authors.forename: Randy F
authors.identifier: 0000-0002-7585-2238
authors.initials: RF
authors.lastname: Lacey
authors.affiliation: Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840 bbinder@utk.edu.
authors.forename: Brad M
authors.identifier: 0000-0002-8172-2034
authors.initials: BM
authors.lastname: Binder
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D005030:Ethylenes / Q000494:pharmacology*; D010861:Fimbriae, Bacterial / Q000187:drug effects / Q000378:metabolism; D055537:Light Signal Transduction / Q000187:drug effects; D009068:Movement; D000071444:Phototaxis / Q000187:drug effects; D011485:Protein Binding / Q000187:drug effects; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*; D046939:Synechocystis / Q000187:drug effects / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D005030:Ethylenes; D011956:Receptors, Cell Surface; C036216:ethylene