Additional file 2.

Amino-acid alignment of secY, rpl36 and rps13 and the rpl36 amino-acid alignment showing the C-terminal extensions and atomic contacts in the ribosome crystal structure. (A) This shows that secY and rps13 from plastids which contain the c-type rpl36 are more similar to secY and rps13 genes from red algae and cyanobacteria than to potential rpl36 donors, Rhodopirellula and proteobacteria. Amino acids that conflict with the consensus amino acid at each position are colored according to the key. The similarity between the c-type rpl36 genes in the haptophyte and cryptophyte plastids and those from Rhodopirellula and proteobacteria is also apparent. Note that rpl36 is flanked by secY and rps13 in plastids of red algal origin, but the c-type rpl36 in bacteria is not flanked by these genes. (B) Amino-acid alignment of c-type and p-type rpl36 genes. Note the three apicomplexans included in the alignment (Plasmodium, Toxoplasma, and Theileria). At the bottom is shown which residues make contact with the 23S rRNA in the ribosome crystal structure of Escherichia coli, which has a p-type rpl36.

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Rice and Palmer BMC Biology 2006 4:31   doi:10.1186/1741-7007-4-31