Primary structure of the DNA polymerase I gene of an alpha-proteobacterium, Rhizobium leguminosarum, and comparison with other family a DNA polymerases
Yp. Huang et al., Primary structure of the DNA polymerase I gene of an alpha-proteobacterium, Rhizobium leguminosarum, and comparison with other family a DNA polymerases, CURR MICROB, 38(6), 1999, pp. 355-359
The structural gene for DNA polymerase I of Rhizobium leguminosarum was det
ermined. The rhizobium DNA polymerase I consists of 1016 amino acid residue
s with a calculated molecular weight of 111, 491 Dalton, The amino acid seq
uence comparison with E. coli DNA polymerase I, Thermus aquaticus DNA polym
erase I, and Rickettsia prowazekii DNA polymerase I showed that, although 5
'-nuclease and DNA polymerase domains are highly conserved, 3' to 5' exonuc
lease domains are much less conserved. While both R. leguminosarum and R. p
rowazekii belong to the alpha subdivision of the Proteobacteria on the basi
s of 16S ribosomal RNA phylogeny, the primary structure of the DNA polymera
se I is quite different; the rhizobium DNA polymerase I has 3' to 5' proofr
eading exonuclease, but the rickettsia DNA polymerase I does not.