title: A novel covalent modification of nitrogenase in a cyanobacterium.
abstract: In extracts of the unicellular cyanobacterium Gloeothece, the Fe-protein of nitrogenase can be separated by SDS-PAGE into two antigenically identifiable components. Unlike the situation in photosynthetic bacteria such as Rhodospirillum rubrum, these two forms do not arise from covalent modification of the protein by ADP-ribosylation. Rather, the Fe-protein of Gloeothece nitrogenase is subjected to modification by palmitoylation.
authors.affiliation: Biochemistry Research Group, School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea, UK. j.r.gallon@swansea.ac.uk
authors.forename: J R
authors.initials: JR
authors.lastname: Gallon
authors.forename: J
authors.initials: J
authors.lastname: Cheng
authors.forename: L J
authors.initials: LJ
authors.lastname: Dougherty
authors.forename: V A
authors.initials: VA
authors.lastname: Gallon
authors.forename: H
authors.initials: H
authors.lastname: Hilz
authors.forename: D M
authors.initials: DM
authors.lastname: Pederson
authors.forename: H M
authors.initials: HM
authors.lastname: Richards
authors.forename: S
authors.initials: S
authors.lastname: Rüggeberg
authors.forename: C J
authors.initials: CJ
authors.lastname: Smith
mesh_terms: D000458:Cyanobacteria / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D008667:Metalloproteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D009591:Nitrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D019308:Palmitic Acid / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D008667:Metalloproteins; D019308:Palmitic Acid; D009591:Nitrogenase