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First published online 12 February 2003
doi: 10.1242/jcs.00333

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Cytoskeletal proteins with N-terminal signal peptides: plateins in the ciliate Euplotes define a new family of articulins

¹ Department of Biological Sciences, University of Maryland Baltimore County (UMBC), Baltimore, MD 21250, USA
² Laboratoire de Biologie Cellulaire 4, Université Paris-Sud, 91405 Orsay, France
³ Biologia MCA, Università di Camerino, 62032 Camerino, Italy
⁴ Kimball Research Institute, New York Blood Center, 310 E. 67th St, New York, NY 10021, USA

^* Author for correspondence (e-mail: kloetzel{at}umbc.edu)

Accepted 18 December 2002

Protistan cells employ a wide variety of strategies to reinforce and give pattern to their outermost cortical layers. Whereas some use common cytoskeletal elements such as microtubules, others are based on novel cytoskeletal proteins that are as-yet-unknown in higher eukaryotes. The hypotrich ciliate Euplotes possesses a continuous monolayer of scales or plates, located within flattened membranous sacs (`alveoli') just below the plasma membrane, and this provides rigidity and form to the cell. Using immunological techniques, the major proteins comprising these `alveolar plates' have been identified and termed -, ß-, and -plateins. The present report describes work leading to the molecular characterization of three plateins, 1 and 2 (predicted M_rs of 61 and 56 kDa) and a ß/ form (M_r=73 kDa). All three proteins have features that are hallmarks of articulins, a class of cytoskeletal proteins that has been identified in the cortex of a wide variety of protistan cells, including certain flagellates, ciliates, dinoflagellates and Plasmodium. Chief among these common features are a prominent primary domain of tandem 12-amino acid repeats, rich in valine and proline, and a secondary domain of fewer, shorter repeating units. However, variations in amino acid use within both primary and secondary repetitive domains, and a much more acidic character (predicted pIs of 4.7-4.9), indicate that the plateins represent the first proteins in a new subclass or family of articulins. This conclusion is supported by another novel feature of the plateins, the presence of a canonical hydrophobic signal peptide at the N-terminus of each derived platein sequence. This correlates well with the final cellular location of the plateins, which are assembled into plates within the membrane-limited alveolar sacs. To our knowledge, this is the first report in any eukaryote of cytoskeletal proteins with such start—transfer sequences. Confocal immunofluorescence microscopy, using antibodies to the plateins as probes, reveals that new alveolar plates (enlarging in cortical zones undergoing morphogenesis) label more faintly than mature parental plates. During plate assembly (or polymerization), the plateins thus appear to exist in a more soluble form.

Key words: Signal sequence, Membrane skeleton, Alveolata, Protist, Epiplasm, Pellicle, Cortical cytoskeleton, Repetitive protein domains, Ciliate expression library

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