Skip to main content
. Author manuscript; available in PMC: 2008 Dec 18.
Published in final edited form as: Mol Cell. 2008 Feb 1;29(2):180–190. doi: 10.1016/j.molcel.2007.11.021

Figure 5. Chimeras of EcoIF2 and IF2mt.

Figure 5

(A) Schematic representation of the domain organization of EcoIF2 and bovine IF2mt. The numbers indicate the amino acid positions. IF2mt lacks the counterparts of EcoIF2 domains I and II. The 37 amino acid insertion conserved in mitochondrial IF2s is indicated by a box.

(B) Alignment of a portion of the sequences of EcoIF2 and bovine IF2mt (shown in bold letters). The identical residues are joined by a dotted line. The 37 amino acid insertion is marked by a bracket and is flanked by regions of high conservation, which were chosen for a swap between the two IF2s.

(C) The sequences of the resulting chimeras are shown.

(D) PCR analysis of ΔinfB::KanR transductants harboring either pACDH-IF2mtΔ37 (lanes 1-3) or pACDH-EcoIF2::37 (lanes 4 and 5) using IF2-FP5, IF2-RP3, IF2-KO-FP, and IF2-KO-RP (Figure 2A) to confirm replacement of infB with KanR. WT stands for wild-type, and M is DNA size marker (λ HindII + HindIII).