title: Immunocytochemical localization of IdiA, a protein expressed under iron or manganese limitation in the mesophilic cyanobacterium Synechococcus PCC 6301 and the thermophilic cyanobacterium Synechococcus elongatus.
abstract: Iron-deficiency-induced protein A (IdiA) with a calculated molecular mass of 35 kDa has previously been shown to be essential under manganese- and iron-limiting conditions in the cyanobacteria Synechococcus PCC 6301 and PCC 7942. Studies of mutants indicated that in the absence of IdiA mainly photosystem II becomes damaged, suggesting that the major function of IdiA is in Mn and not Fe metabolism (Michel et al. 1996, Microbiology 142: 2635-2645). To further elucidate the function of IdiA, the immunocytochemical localization of IdiA in the cell was examined. These investigations provided evidence that under mild Fe deficiency IdiA is intracellularly localized and is mainly associated with the thylakoid membrane in Synechococcus PCC 6301. The protein became distributed throughout the cell under severe Fe limitation when substantial morphological changes had already occurred. For additional verification of a preferential thylakoid membrane association of IdiA, these investigations were extended to the thermophilic Synechococcus elongatus. In this cyanobacterium Mn deficiency could be obtained more rapidly than in the mesophilic Synechococcus PCC 6301 and PCC 7942, and the thylakoid membrane structure proved to be more stable under limiting growth conditions. The immunocytochemical investigations with this cyanobacterium clearly supported a thylakoid membrane association of IdiA. In addition, evidence was obtained for a localization of IdiA on the cytoplasmic side of the thylakoid membrane. All available data support a function of IdiA as an Mn-binding protein that facilitates transport of Mn via the thylakoid membrane into the lumen to provide photosystem II with Mn. A possible explanation for the observation that IdiA was not only expressed under Mn deficiency but also under Fe deficiency is given in the discussion.
authors.affiliation: Morphologie der Pflanzen und Feinbau der Zelle, Universität Bielefeld, Germany.
authors.forename: K P
authors.initials: KP
authors.lastname: Michel
authors.forename: P
authors.initials: P
authors.lastname: Exss-Sonne
authors.forename: G
authors.initials: G
authors.lastname: Scholten-Beck
authors.forename: U
authors.initials: U
authors.lastname: Kahmann
authors.forename: H G
authors.initials: HG
authors.lastname: Ruppel
authors.forename: E K
authors.initials: EK
authors.lastname: Pistorius
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D000458:Cyanobacteria / Q000254:growth & development / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D007425:Intracellular Membranes / Q000378:metabolism / Q000648:ultrastructure; D007501:Iron / Q000378:metabolism*; D033862:Iron-Binding Proteins; D008345:Manganese / Q000378:metabolism*; D008854:Microscopy, Electron
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; C102679:IdiA protein, Synechococcus; D033862:Iron-Binding Proteins; D008345:Manganese; D007501:Iron