2003
DOI: 10.1242/jcs.00517
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Plastid ultrastructure defines the protein import pathway in dinoflagellates

Abstract: Eukaryotic cells contain a variety of different compartments that are distinguished by their own particular function and characteristic set of proteins. Protein targeting mechanisms to organelles have an additional layer of complexity in algae, where plastids may be surrounded by three or four membranes instead of two as in higher plants. The mechanism of protein import into dinoflagellates plastids, however, has not been previously described despite the importance of plastid targeting in a group of algae resp… Show more

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Cited by 104 publications
(146 citation statements)
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“…To confirm that the C. velia Rubisco gene is nucleus-encoded, we used 3′ and 5′ RACE to show the transcript is polyadenylated and encodes an N-terminal extension with characteristics required for plastid-targeting. Both features were confirmed, and the N-terminal extension was found to encode a readily identifiable signal peptide (P = 0.998 in SignalP-HMM) followed by a positively charged region, features consistent with the bipartite leader required for plastid-targeting in apicomplexans and dinoflagellates (22,23).…”
Section: Ccmp3155mentioning
confidence: 72%
“…To confirm that the C. velia Rubisco gene is nucleus-encoded, we used 3′ and 5′ RACE to show the transcript is polyadenylated and encodes an N-terminal extension with characteristics required for plastid-targeting. Both features were confirmed, and the N-terminal extension was found to encode a readily identifiable signal peptide (P = 0.998 in SignalP-HMM) followed by a positively charged region, features consistent with the bipartite leader required for plastid-targeting in apicomplexans and dinoflagellates (22,23).…”
Section: Ccmp3155mentioning
confidence: 72%
“…An altered ERAD-related machinery involved in the regular transport of properly folded proteins out of the ER and into the periplastidic compartment was therefore suggested (Sommer et al 2007). Meanwhile considerable knowledge about the presequence structure of nucleus encoded plastid targeted proteins from diatoms, cryptophytes and dinoflagellates was gained (Apt et al 2002;Gould et al 2006a;Kilian and Kroth 2005;Nassoury et al 2003;Patron et al 2005, this study), remarkably, the detailed import process of proteins targeted to the plastids via the ER remains largely unknown.…”
Section: Discussionmentioning
confidence: 89%
“…Presequences of nucleus encoded plastid proteins consist of a signal peptide followed by a transit peptide-like domain (Pancic and Strotmann 1993). The functionality of both domains was proven individually in vitro in heterologous import systems (Bhaya and Grossman 1991;Chaal and Green 2005;Ishida et al 2000;Lang et al 1998;Nassoury et al 2003;Wastl and Maier 2000), and previous studies in the diatom Phaeodactylum tricornutum demonstrated the in vivo functionality of native plastid presequences:GFP fusion proteins (Apt et al 2002). Interestingly, also heterologous presequences from the diatom Odontella sinensis Kroth et al 2005) or from the dinoflagellate Symbiodinium sp.…”
Section: Introductionmentioning
confidence: 96%
“…from algae with primary plastids through secondary endosymbioses (19)] were shown to passage through the Golgi (20,21). Plastid proteins synthesized in the cytoplasm of these algal cells have Nterminal, bipartite presequences composed of an ER-targeting signal [signal peptide (SP)] and a TP-like sequence.…”
Section: Discussionmentioning
confidence: 99%