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Reciprocal Regulation of Protein Synthesis and Carbon Metabolism for Thylakoid Membrane Biogenesis

Figure 2

Three homologous dihydrolipoamide-acetyltransferases (DLAs) in C. reinhardtii.

Multiple alignment of deduced amino acid sequences of the three DLA genes of C. reinhardtii along with Synechocystis sp. PCC 6803, human, S. cerevisiae, and A. thaliana sequences. Conserved residues are shaded in black, similar residues in grey. The sequences were aligned with ClustalW, manually edited and visualized using GeneDoc [81],[82]. The predicted chloroplast transit peptide of CrDLA2 has a length of 30 amino acids and is indicated by scissors. Functional domains are depicted below the sequences. Boxed regions in the DLA2 amino acid sequence correspond to peptides identified by mass spectrometry. Arrowheads indicate the amino acids fused to GFP (Figure 3B). Accession numbers are as follows: C. reinhardtii CrDLA1 (EDP01882), CrDLA3 (XP_001696403), CrDLA2 (model: au5.g10333 annotated in JGI v4; Joint Genome Institute; http://genome.jgi-psf.org/Chlre4/Chlre4.home.html); A. thaliana At-mtE2 (LTA3, AAV97810), At-cpE2 (LTA2, NP_189215); Synechocystis sp. 6803 Syn-E2 (sll1841, NP_441936); H. sapiens Hs-E2 (DLAT, NM_001931); and S. cerevisiae Sc-E2 (Lat1, NP_014328).

Figure 2

doi: https://doi.org/10.1371/journal.pbio.1001482.g002