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Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | FEBS Letters, 484, 2000, 1, S. 43-47 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Szilvay, Anne Marie Stern, Beate Blichenberg, Arne Helland, Dag E. Szilvay, Anne Marie Stern, Beate Blichenberg, Arne Helland, Dag E. |
|---|---|
| author |
Szilvay, Anne Marie Stern, Beate Blichenberg, Arne Helland, Dag E. |
| spellingShingle |
Szilvay, Anne Marie Stern, Beate Blichenberg, Arne Helland, Dag E. FEBS Letters Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
szilvay, anne marie |
| spelling |
Szilvay, Anne Marie Stern, Beate Blichenberg, Arne Helland, Dag E. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(00)02113-x <jats:p>Four monoclonal antibodies (MAbs) recognizing HIV‐1 reverse transcriptase (RT) were shown here to cross‐react with the β′ subunit of <jats:italic>Escherichia coli</jats:italic> 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.</jats:p> Structural and functional similarities between HIV‐1 reverse transcriptase and the <i>Escherichia coli</i> RNA polymerase β′ subunit FEBS Letters |
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| title |
Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_unstemmed |
Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_full |
Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_fullStr |
Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_full_unstemmed |
Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_short |
Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_sort |
structural and functional similarities between hiv‐1 reverse transcriptase and the <i>escherichia coli</i> rna polymerase β′ subunit |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
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http://dx.doi.org/10.1016/s0014-5793(00)02113-x |
| publishDate |
2000 |
| physical |
43-47 |
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<jats:p>Four monoclonal antibodies (MAbs) recognizing HIV‐1 reverse transcriptase (RT) were shown here to cross‐react with the β′ subunit of <jats:italic>Escherichia coli</jats:italic> 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.</jats:p> |
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| author | Szilvay, Anne Marie, Stern, Beate, Blichenberg, Arne, Helland, Dag E. |
| author_facet | Szilvay, Anne Marie, Stern, Beate, Blichenberg, Arne, Helland, Dag E., Szilvay, Anne Marie, Stern, Beate, Blichenberg, Arne, Helland, Dag E. |
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| description | <jats:p>Four monoclonal antibodies (MAbs) recognizing HIV‐1 reverse transcriptase (RT) were shown here to cross‐react with the β′ subunit of <jats:italic>Escherichia coli</jats:italic> 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.</jats:p> |
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| imprint | Wiley, 2000 |
| imprint_str_mv | Wiley, 2000 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 43-47 |
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| series | FEBS Letters |
| source_id | 49 |
| spelling | Szilvay, Anne Marie Stern, Beate Blichenberg, Arne Helland, Dag E. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(00)02113-x <jats:p>Four monoclonal antibodies (MAbs) recognizing HIV‐1 reverse transcriptase (RT) were shown here to cross‐react with the β′ subunit of <jats:italic>Escherichia coli</jats:italic> 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.</jats:p> Structural and functional similarities between HIV‐1 reverse transcriptase and the <i>Escherichia coli</i> RNA polymerase β′ subunit FEBS Letters |
| spellingShingle | Szilvay, Anne Marie, Stern, Beate, Blichenberg, Arne, Helland, Dag E., FEBS Letters, Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_full | Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_fullStr | Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_full_unstemmed | Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_short | Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| title_sort | structural and functional similarities between hiv‐1 reverse transcriptase and the <i>escherichia coli</i> rna polymerase β′ subunit |
| title_unstemmed | Structural and functional similarities between HIV‐1 reverse transcriptase and the Escherichia coli RNA polymerase β′ subunit |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/s0014-5793(00)02113-x |