Epiplasts: Membrane Skeletons and Epiplastin Proteins in Euglenids, Glaucophytes, Cryptophytes, Ciliates, Dinoflagellates, and Apicomplexans.

作者: Ursula Goodenough , Robyn Roth , Thamali Kariyawasam , Amelia He , Jae-Hyeok Lee

DOI: 10.1128/MBIO.02020-18

关键词:

摘要: ABSTRACT Animals and amoebae assemble actin/spectrin-based plasma membrane skeletons, forming what is often called the cell cortex, whereas euglenids alveolates (ciliates, dinoflagellates, apicomplexans) have been shown to a thin, viscoelastic, actin/spectrin-free skeleton, here epiplast. Epiplasts include class of proteins, epiplastins, with head/medial/tail domain organization, whose medial domains characterized in previous studies by their low-complexity amino acid composition. We identified two additional features domains: strong enrichment acid/base dyads predicted β-strand/random coil secondary structure. These served identify members unicellular eukaryotic radiations—the glaucophytes cryptophytes—as well as euglenids. analyzed composition structure 219 epiplastin sequences used quick-freeze deep-etch electron microscopy visualize epiplasts cryptophytes. define epiplastins proteins encoded organisms that epiplasts, but epiplastin-like unknown function, are also Insecta, Basidiomycetes, Caulobacter genomes. discuss diverse cellular traits supported propose evolutionary scenarios consonant distribution extant eukaryotes. IMPORTANCE Membrane skeletons associate inner surface provide support for fragile lipid bilayer an elastic framework itself. Several radiations, including animals, organize such using actin/spectrin four major radiations organisms, disease-causing parasites Plasmodium, known construct alternative essential skeleton (the epiplast) we term epiplastins. present images microscopy. analyze in-depth overview analysis posited roles organization parasite infection. An understanding epiplast assembly may suggest therapeutic approaches combat infectious agents Plasmodium engineering useful viscoelastic biofilms.

参考文章(180)
G. Benjamin Bouck, Huan Ngo, Cortical Structure and Function in Euglenoids with Reference to Trypanosomes, Ciliates, and Dinoflagellates International Review of Cytology-a Survey of Cell Biology. ,vol. 169, pp. 267- 318 ,(1996) , 10.1016/S0074-7696(08)61988-9
Brooke Anderson-White, Josh R. Beck, Chun-Ti Chen, Markus Meissner, Peter J. Bradley, Marc-Jan Gubbels, Cytoskeleton assembly in Toxoplasma gondii cell division International Review of Cell and Molecular Biology. ,vol. 298, pp. 1- 31 ,(2012) , 10.1016/B978-0-12-394309-5.00001-8
Eliane Porchet, G�rard Torpier, Etude du germe infectieux de Sarcocystis tenella et Toxoplasma gondii par la technique du cryodécapage Parasitology Research. ,vol. 54, pp. 101- 124 ,(1977) , 10.1007/BF00380795
Tze-tuan Chen, Research in Protozoology ,(1967)
Bin Wang, Wen Yang, Joanna McKittrick, Marc André Meyers, Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration Progress in Materials Science. ,vol. 76, pp. 229- 318 ,(2016) , 10.1016/J.PMATSCI.2015.06.001
Lenita C. Morrill, Alfred R. Loeblich, Ultrastructure of the Dinoflagellate Amphiesma International Review of Cytology. ,vol. 82, pp. 151- 180 ,(1983) , 10.1016/S0074-7696(08)60825-6
Norman E. Williams, Pierre E. Vaudaux, Lars Skriver, Cytoskeletal proteins of the cell surface in Tetrahymena Experimental Cell Research. ,vol. 123, pp. 311- 320 ,(1979) , 10.1016/0014-4827(79)90473-7
Marjorie Linares, Dee Carter, Sven B. Gould, Chromera et al.: Novel Photosynthetic Alveolates and Apicomplexan Relatives Springer Vienna. pp. 183- 196 ,(2014) , 10.1007/978-3-7091-1303-5_10
John C. Wootton, Scott Federhen, Analysis of compositionally biased regions in sequence databases. Methods in Enzymology. ,vol. 266, pp. 554- 571 ,(1996) , 10.1016/S0076-6879(96)66035-2
Carol A. Sattler, L. Andrew Staehelin, Oral cavity of Tetrahymena pyriformis Journal of Ultrastructure Research. ,vol. 66, pp. 132- 150 ,(1979) , 10.1016/S0022-5320(79)90130-8