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Updated: Aug 8, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
Structural and functional similarities between HIV-1 reverse transcriptase and the Escherichia coli RNA polymerase
A M Szilvay1, B Stern, A Blichenberg
1Department of Molecular Biology, University of Bergen, HIB, P.O. Box 7800, N-5020, Bergen, Norway. anne.szilvay@mbi.uib.no
Abstract:
Four monoclonal antibodies (MAbs) recognizing HIV-1 reverse transcriptase (RT) were shown here to cross-react with the beta' subunit of Escherichia coli RNA polymerase (RNAP). The anti-RT MAbs bind to a peptide comprising residues 294-305 of the RT amino acid sequence. Computer analyses revealed sequence similarity between this peptide and two regions of the RNAP beta' subunit. MAb-binding studies using RT mutants suggested that the epitope is located to amino acids 652-663 of the beta' sequence. One of the MAbs which inhibited the polymerase activity of RT also mediated a dose dependent inhibition of the RNAP activity.
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