Skip to main content
Figure 1 | Virology Journal

Figure 1

From: Influence of the RNase H domain of retroviral reverse transcriptases on the metal specificity and substrate selection of their polymerase domains

Figure 1

(A) Schematic representation showing the polymerase connection and RNase H domains of wild-type RTs and their chimeric derivatives. Swapping of the RNase H domain between the wild-type HIV-1 RT and MuLV RT to construct their chimeric derivatives is shown by arrows. (B) Coomassie Blue stained SDS polyacrylamide gel of the wild-type enzymes and their chimeric derivatives. An aliquot of purified chimeric enzymes, M-pol, wild-type p66/66 HIV-1 RT, and MuLV RT was resolved by SDS-PAGE; protein bands were visualized by Coomassie blue staining. In the wild-type HIV-1 RT lane, the minor band seen at the 51 kD position may have been generated by proteolytic cleavage during purification. The positions corresponding to 66 kD and 51 kD are indicated on the left

Back to article page