van Teeseling, Muriel C. F. and de Almeida, Naomi M. and Klingl, Andreas and Speth, Daan R. and Op den Camp, Huub J. M. and Rachel, Reinhard and Jetten, Mike S. M. and van Niftrik, Laura (2014) A New Addition to the Cell Plan of Anammox Bacteria: "Candidatus Kuenenia stuttgartiensis" Has a Protein Surface Layer as the Outermost Layer of the Cell. JOURNAL OF BACTERIOLOGY, 196 (1). pp. 80-89. ISSN 0021-9193, 1098-5530
Full text not available from this repository. (Request a copy)Abstract
Anammox bacteria perform anaerobic ammonium oxidation (anammox) and have a unique compartmentalized cell consisting of three membrane-bound compartments (from inside outwards): the anammoxosome, riboplasm, and paryphoplasm. The cell envelope of anammox bacteria has been proposed to deviate from typical bacterial cell envelopes by lacking both peptidoglycan and a typical outer membrane. However, the composition of the anammox cell envelope is presently unknown. Here, we investigated the outermost layer of the anammox cell and identified a proteinaceous surface layer (S-layer) (a crystalline array of protein subunits) as the outermost component of the cell envelope of the anammox bacterium "Candidatus Kuenenia stuttgartiensis." This is the first description of an S-layer in the phylum of the Planctomycetes and a new addition to the cell plan of anammox bacteria. This S-layer showed hexagonal symmetry with a unit cell consisting of six protein subunits. The enrichment of the S-layer from the cell led to a 160-kDa candidate protein, Kustd1514, which has no homology to any known protein. This protein is present in a glycosylated form. Antibodies were generated against the glycoprotein and used for immunogold localization. The antiserum localized Kustd1514 to the S-layer and thus verified that this protein forms the "Ca. Kuenenia stuttgartiensis" S-layer.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ANAEROBIC AMMONIUM OXIDATION; GRAM-POSITIVE BACTERIA; S-LAYER; OXIDIZING BACTERIA; MASS-SPECTROMETRY; BUDDING BACTERIA; WALL POLYMERS; GLYCOSYLATION; MECHANISM; SEQUENCE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Reinhard Rachel |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 29 Nov 2019 11:55 |
| Last Modified: | 29 Nov 2019 11:55 |
| URI: | https://pred.uni-regensburg.de/id/eprint/11048 |
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