Supplementary material for Frye et al., Proc. Natl. Acad. Sci. USA, 10.1073/pnas.011405198

Supplemental Figure 6

Fig. 6.

 Full-length alignment of EDR1 homologous proteins. Proteins were aligned by using the default parameters of CLUSTAL X, a Macintosh version of the CLUSTAL W program (1). The alignment file produced by CLUSTAL X was formatted by using the BOXSHADE www server (http://www.ch.embnet.org/software/BOX_form.html). White type on a black background indicates a residue that is identical in at least half of the proteins shown, whereas a gray background indicates conservative substitutions as defined by the BOXSHADE 3.21 default parameters. Asterisks indicate residues that are conserved in nearly all protein kinases (2). Arrows indicate regions conserved in the tomato and rice EDR1 orthologs but divergent in paralogs. These were used to design degenerate oligonucleotide primers for amplification of EDR1 orthologs from other species. Putative EDR1 and CTR1 orthologs are preceded by a two-letter prefix to indicate species of origin: Hv, Hordeum vulgare (barley; accession no. AF305912), Os, Oryza sativa (rice; accession no. AF305911), Le, Lycopersicon esculentum (tomato; accession no. AJ005077), At, Arabadopsis thaliana (accession no. AF305913). Accession no. AC034107 refers to BAC DNA sequence, from which we derived the indicated protein sequence, using the AtEDR1 and AtCTR1 sequences as guides.

References:

  1. Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994) Nucleic Acids Res. 22, 4673–4680.
  2. Hanks, S. K. & Quinn, A. M. (1991) Methods Enzymol. 200, 38–62.