Rhodopsins build up the birefringent bodies of the dinoflagellate Oxyrrhis marina.
The ultrastructure of the birefringent bodies of the dinoflagellate Oxyrrhis marina was investigated by transmission electron microscopy. Ultrathin sectioning revealed that the bodies consist of highly ordered and densely packed lamellae, which show a regular striation along their longitudinal axis....
| Publicado en: | Protoplasma Vol. 259; no. 4; pp. 1047 - 1061 |
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| Autores principales: | , , |
| Formato: | Journal Article |
| Publicado: |
Springer Nature
Jul2022
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=157411127&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 157411127 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 0033183X 2CF jtl: Protoplasma issn: 0033183X maglogo: N pubinfo: dt: Jul2022 vid: 259 iid: 4 pid: 237 pub: Springer Nature place: New York, New York artinfo: ui: 157411127 153394089 10.1007/s00709-021-01717-y 157411127 ppf: 1047 ppct: 14 formats: fmt: – @attributes: type: T – @attributes: type: P tig: atl: Rhodopsins build up the birefringent bodies of the dinoflagellate Oxyrrhis marina. aug: au: Rhiel, Erhard Hoischen, Christian Westermann, Martin affil: Plankton Ecology, Institute for Chemistry and Biology of the Marine Environment, Carl Von Ossietzky University Oldenburg, Carl–von–Ossietzky–Straße 9–11, D–26129, Oldenburg, Germany sug: ab: The ultrastructure of the birefringent bodies of the dinoflagellate Oxyrrhis marina was investigated by transmission electron microscopy. Ultrathin sectioning revealed that the bodies consist of highly ordered and densely packed lamellae, which show a regular striation along their longitudinal axis. A lattice distance of 6.1 nm was measured for the densely packed lamellae by FFT (Fast Fourier Transformation) analysis. In addition, a rather faint and oblique running striation was registered. Lamellae sectioned rather oblique or almost close to the surface show a honeycombed structure with a periodicity of 7.2–7.8 nm. Freeze-fracture transmission electron microscopy revealed that the lamellae are composed of highly ordered, crystalline arrays of particles. Here, FFT analysis resulted in lattice distances of 7.0–7.6 nm. Freeze-fracture transmission electron microscopy further revealed that the bodies remained intact after cell rupture followed by ascending flotation of the membrane fractions on discontinuous sucrose gradients. The birefringent bodies most likely are formed by evaginations of membranes, which separate the cytoplasm from the food vacuoles. Distinct, slightly reddish-colored areas, which resembled the birefringent bodies with respect to size and morphology, were registered by bright field light microscopy within Oxyrrhis marina cells. An absorbance maximum at 540 nm was registered for these areas, indicating that they are composed of rhodopsins. This was finally proven by immuno-transmission electron microscopy, as antisera directed against the C-terminal amino acid sequences of the rhodopsins AEA49880 and ADY17806 intensely immunolabeled the birefringent bodies of Oxyrrhis marina. pubtype: Academic Journal doctype: Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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