The land plant Arabidopsis thaliana contains three closely related nuclear
genes encoding phage-type RNA polymerases (RpoT;1, RpoT;2 and RpoT;3). The
gene products of RpoT;1 and RpoT;3 have previously been shown to be importe
d into mitochondria and chloroplasts, respectively. Here we show that the t
ransit peptide of RpoT;2 possesses dual targeting properties. Transient exp
ression assays in tobacco protoplasts as well as stable transformation of A
rabidopsis plants demonstrate efficient targeting of fusion peptides consis
ting of the N-terminus of RpoT;2 joined to green fluorescent protein to bot
h organelles. Thus, RpoT;2 might be the first RNA polymerase shown to trans
cribe genes in two different genomes. RNA polymerase activity of recombinan
t RpoT;2 is uneffected by the inhibitor tagetin, qualifying the gene produc
t of RpoT;2 as a phage-type polymerase.