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Summary
| Description |
English: Membrane structre of an algal chromista cell (myzozoa). These originated by secondary intracellular enslavement of a red algal plant cell. Both target nuclear-coded proteins to plastids by transit peptides (TPs) recognised by outer membrane (OM, blue) Toc receptors and to mitochondria (enslaved α-proteobacteria) by topogenic sequences recognised by OM Tom receptors. For clarity, peroxisomes and lysosomes omitted. Myzozoa lack periplastid ribosomes, phycobilins, and nucleomorph DNA; thylakoids are stacked in threes; PPM (present in Apicomplexa—red dashed line; lost in Dinozoa) and plastids are not within the rough ER. The original phagosome membrane (now epiplastid membrane, EpM) remains smooth and receives vesicles (V) containing nucleus-encoded plastid proteins from the Golgi. Dinozoa lack PR, but Apicomplexa have a likely homologue (not shown). |
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| Source | Fig. 3c at https://link.springer.com/article/10.1007/s00709-017-1147-3 Kingdom Chromista and its eight phyla: a new synthesis emphasising periplastid protein targeting, cytoskeletal and periplastid evolution, and ancient divergences. In: Protoplasma 255,pages 297–357, doi:10.1007/s00709-017-1147-3 | |||
| Author | Thomas Cavalier-Smith (caption slightly moved, digitylly enhanced) | |||
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
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| current | 14:33, 8 August 2022 | | 620 × 618 (60 KB) | Ernsts | Uploaded a work by Thomas Cavalier-Smith from Fig. 3+6 at https://link.springer.com/article/10.1007/s00709-017-1147-3 Kingdom Chromista and its eight phyla: a new synthesis emphasising periplastid protein targeting, cytoskeletal and periplastid evolution, and ancient divergences. In: Protoplasma 255, doi:10.1007/s00709-017-1147-3 with UploadWizard |
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