title: Heteromultimerization of prokaryotic bacterial cyclic nucleotide-gated (bCNG) ion channels, members of the mechanosensitive channel of small conductance (MscS) superfamily.
abstract: Traditionally, prokaryotic channels are thought to exist as homomultimeric assemblies, while many eukaryotic ion channels form complex heteromultimers. Here we demonstrate that bacterial cyclic nucleotide-gated channels likely form heteromultimers in vivo. Heteromultimer formation is indicated through channel modeling, pull-down assays, and real-time polymerase chain reaction analysis. Our observations demonstrate that prokaryotic ion channels can display complex behavior and regulation akin to that of their eukaryotic counterparts.
authors.affiliation: Department of Chemistry, Washington University in St. Louis , St. Louis, Missouri 63112, United States.
authors.forename: Hannah R
authors.initials: HR
authors.lastname: Malcolm
authors.forename: Yoon-Young
authors.initials: YY
authors.lastname: Heo
authors.forename: Donald E
authors.initials: DE
authors.lastname: Elmore
authors.forename: Joshua A
authors.initials: JA
authors.lastname: Maurer
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D054815:Cyclic Nucleotide-Gated Cation Channels / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D046939:Synechocystis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D054815:Cyclic Nucleotide-Gated Cation Channels; D021122:Protein Subunits; D011994:Recombinant Proteins