Protein introns are recently discovered genetic elements whose interve
ning sequences are removed from a precursor protein by an unusual prot
ein splicing reaction. This involves the excision of a central spacer
molecule, the protein intron, and the religation of the amino- and car
boxy-terminal fragments of the precursor. The recA gene of Mycobacteri
um tuberculosis contains one such element and we now show that the oth
er major mycobacterial pathogen, Mycobacterium leprae, also possesses
a protein intron in its recA, although other mycobacterial recA genes
do not. However, these two protein introns are different in size, sequ
ence and location of insertion of their coding sequences into the recA
s of M.tuberculosis and M.leprae, indicating that acquisition of the p
rotein introns has occurred independently in the two species, and thus
suggesting that there has been selection for splicing in the maturati
on of RecA in the pathogenic mycobacteria. The M.leprae protein intron
provides an example of conditional protein splicing, splicing occurri
ng in M.leprae itself but not when expressed in Escherichia coli, unli
ke most previously described protein introns. These observations sugge
st that protein introns may perform a function for their host, rather
than being just selfish elements.