An unusual mechanism of bacterial gene expression revealed for the RNase P protein of Thermus strains -- Data Supplement - Supporting Information -- Proceedings of the National Academy of Sciences

Supporting information for Feltens et al. (2003) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.0931462100

Fig. 6.
(A) Time courses of proteolytic processing of C5₅₁ and C5₁ in a T. thermophilus cytosolic extract at 70ºC detected by Western blot analyses using the C5₈₇-specific antiserum. The position of the relatively stable processing product C5₆₄ is marked by the arrow. (B) Incubation of the recombinant C5₁ with an E. coli cytosolic extract for 90 min at 37ºC. M, prestained marker proteins with sizes (in kDa) indicated. (C) Alignment of C5 proteins from six Thermus species with RNase P proteins from S. aureus (Sau) and B. subtilis (Bsu). Amino acids in B. subtilis and S. aureus RNase P proteins similar or identical to those found at the corresponding location in Thermus species are marked by white letters on gray background; amino acid identities that vary among Thermus species are marked by white letters on black background. The N termini of the recombinant proteins C5₅₁, C5₆₄, and C5₈₇ (minus their His tags) are indicated. Secondary structure elements for B. subtilis and S. aureus are indicated by horizontal boxes (black, α-helices; open, β-strands).