title: Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester.
abstract: This study describes the characterization of orf358, an open reading frame of previously unidentified function, in the purple bacterium Rubrivivax gelatinosus. A strain in which orf358 was disrupted exhibited a phenotype similar to the wild type under photosynthesis or low-aeration respiratory growth conditions. In contrast, under highly aerated respiratory growth conditions, the wild type still produced bacteriochlorophyll a (Bchl a), while the disrupted strain accumulated a compound that had the same absorption and fluorescence emission spectra as Mg-protoporphyrin but was less polar, suggesting that it was Mg-protoporphyrin monomethylester (MgPMe). These data indicated a blockage in Bchl a synthesis at the oxidative cyclization stage and implied the coexistence of two different mechanisms for MgPMe cyclization in R. gelatinosus, an anaerobic mechanism active under photosynthesis or low oxygenation and an aerobic mechanism active under high-oxygenation growth conditions. Based on these results as well as on sequence analysis indicating the presence of conserved putative binuclear-iron-cluster binding motifs, the designation of orf358 as acsF (for aerobic cyclization system Fe-containing subunit) is proposed. Several homologs of AcsF were found in a wide range of photosynthetic organisms, including Chlamydonomas reinhardtii Crd1 and Pharbitis nil PNZIP, suggesting that this aerobic oxidative cyclization mechanism is conserved from bacteria to plants.
authors.affiliation: Laboratoire de Génétique des Bactéries Photosynthétiques, Centre de Génétique Moléculaire, UPR2167 associée à l'Université Pierre-et-Marie-Curie, CNRS, 91198 Gif-sur-Yvette Cedex, France.
authors.forename: Violaine
authors.initials: V
authors.lastname: Pinta
authors.forename: Martine
authors.initials: M
authors.lastname: Picaud
authors.forename: Françoise
authors.initials: F
authors.lastname: Reiss-Husson
authors.forename: Chantal
authors.initials: C
authors.lastname: Astier
mesh_terms: D000332:Aerobiosis; D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins; D003001:Cloning, Molecular; D017124:Conserved Sequence; D005816:Genetic Complementation Test; D007501:Iron; D008667:Metalloproteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010101:Oxygen Consumption / Q000235:genetics; D010641:Phenotype; D010788:Photosynthesis / Q000235:genetics; D020161:Physical Chromosome Mapping; D010860:Pigments, Biological / Q000032:analysis; D011524:Protoporphyrins / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
chemical_list: C446049:AcsF protein, Rubrivivax gelatinosus; D001426:Bacterial Proteins; D008667:Metalloproteins; D010860:Pigments, Biological; D011524:Protoporphyrins; C033434:protoporphyrin IX monomethyl ester; D007501:Iron