The Presence and Localization of Thioredoxins in Diatoms, Unicellular Algae of Secondary Endosymbiotic Origin Weber Till , Gruber Ansgar , Kroth Peter.

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The Presence and Localization of Thioredoxins in Diatoms, Unicellular Algae of Secondary Endosymbiotic Origin Weber Till , Gruber Ansgar , Kroth Peter G. Molecular Plant Volume 2, Issue 3, Pages 468-477 (May 2009) DOI: 10.1093/mp/ssp010 Copyright © 2009 The Authors. All rights reserved. Terms and Conditions

Figure 1 Presence and Localization of Thioredoxins and Thioredoxin Reducing Enzymes in the Diatom Phaeodactylum tricornutum as Deduced from the Genome Annotation and the Localization of GFP:Fusion Proteins. M, mitochondrium; N, nucleus; C, cytosol; P, plastid; PPS, periplastidic space; Trx, different thioredoxin isoforms; FTR, ferredoxin thioredoxin reductase; NTR, NADPH depending thioredoxin reductase; NTRC, NTR containing N-terminal thioredoxin domain. Molecular Plant 2009 2, 468-477DOI: (10.1093/mp/ssp010) Copyright © 2009 The Authors. All rights reserved. Terms and Conditions

Figure 2 Comparison of Thioredoxin Sequences. A) Maximum likelihood tree using PhyML based on 40 thioredoxin sequences from diatoms and plant homologs. Numbers at nodes of subtrees correspond to bootstrap values greater than 50%. Sequences established in this study are highlighted in gray boxes. The Phaeodactylum tricornutum (Pt) and Thalassiosira pseudonana (Tp) accession numbers corresponded to Protein IDs from the JGI database, the Arabidopsis thaliana (At) accession numbers to the NCBI database. The diatom proteins Pt_TrxY_56644, Tp_TrxY_30505, and Tp_TrxY_19977 represent thioredoxin-like proteins with extended N-termini. Plant thioredoxin o corresponds to EST sequences as described in Laloi et al. (2001). The translation of the following EST contigs are used: Gossypium hirsutum (Gs) (GenBank ESTs AI725806, AI941321), Glycine max (Gm) (AW423678, AW234806, BE210498, AI941321), Solanum lycopersicum (Sl) (BE462179, AW037483, AW037392, BE433326), Zea mays (Zm) (BE345397, AI668273, BE519105, AI737410, BE050128), Oryza sativa (Os) (C27892, AU100897). B) Alignment of the conserved motif containing the regulatory cysteines of the thioredoxins identified in P. tricornutum and T. pseudonana. The numbers refer to the respective protein IDs. Molecular Plant 2009 2, 468-477DOI: (10.1093/mp/ssp010) Copyright © 2009 The Authors. All rights reserved. Terms and Conditions

Figure 3 Presequence Structures and EGFP Fusion Constructs Used in this Study. NTR, NADPH depending thioredoxin reductase; NTRC, NTR containing N-terminal thioredoxin domain; TrxH, thioredoxin h; FTR, ferredoxin thioredoxin reductase; TrxF, thioredoxin f; TrxM, thioredoxin m; TrxY, thioredoxin y; TrxO, thioredoxin o; number in brackets, protein ID; bold letters, predicted signal peptides by Hidden Markov models (Nielsen et al., 1999); underlined, predicted transit peptides; italics, mature protein; gray boxes, predicted signal peptide cleavage site; black box, EGFP. Molecular Plant 2009 2, 468-477DOI: (10.1093/mp/ssp010) Copyright © 2009 The Authors. All rights reserved. Terms and Conditions

Figure 4 Localization of Presequence:GFP Fusion Proteins as Described in Figure 3, Expressed in P. tricornutum. First column: light microscopical images using Normarski differential interference contrast (DIC). Second column: chlorophyll autofluorescence. Third column: GFP fluorescence. Fourth column: merged channels. The scale bars represent 10 μm. Molecular Plant 2009 2, 468-477DOI: (10.1093/mp/ssp010) Copyright © 2009 The Authors. All rights reserved. Terms and Conditions