Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit

FEBS Letters

Helland, Dag E.¹  Stern, Beate¹  Szilvay, Anne Marie¹  Blichenberg, Arne¹ 

[1] Department of Molecular Biology, University of Bergen, HIB, P.O. Box 7800, N-5020 Bergen, Norway

关键词: Escherichia coli RNA polymerase;    HIV-1 reverse transcriptase;    Monoclonal antibody;    Cross-reactivity;    Sequence comparison;    RT;    reverse transcriptase;    RNAP;    RNA polymerase;    MAb;    monoclonal antibody;    HIV-1;    human immunodeficiency virus type 1;    ds;    double-stranded;    ss;    single-stranded;    aa;    amino acid(s);    3D;    three dimensional;    ELISA;    enzyme-linked immunosorbent assay;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(00)02113-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Four monoclonal antibodies (MAbs) recognizing HIV-1 reverse transcriptase (RT) were shown here to cross-react with the β′ 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 β′ subunit. MAb-binding studies using RT mutants suggested that the epitope is located to amino acids 652–663 of the β′ sequence. One of the MAbs which inhibited the polymerase activity of RT also mediated a dose dependent inhibition of the RNAP activity.

【 授权许可】

Unknown