Structural and functional similarities between HIV-1 reverse transcriptaseand the Escherichia coli RNA polymerase beta ' subunit

Citation
Am. Szilvay et al., Structural and functional similarities between HIV-1 reverse transcriptaseand the Escherichia coli RNA polymerase beta ' subunit, FEBS LETTER, 484(1), 2000, pp. 43-47
Citations number
29
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
484
Issue
1
Year of publication
2000
Pages
43 - 47
Database
ISI
SICI code
0014-5793(20001027)484:1<43:SAFSBH>2.0.ZU;2-Y
Abstract
Four monoclonal antibodies (MAbs) recognizing HIV-1 reverse transcriptase ( RT) were shown here to crossreact with the beta' subunit of Escherichia col i RNA polymerase (RNAP). The anti-RT MAbs bind to a peptide comprising resi dues 294-305 of the RT amino acid sequence, Computer analyses revealed sequ ence similarity between this peptide and two regions of the RNAP beta' subu nit, MAb-binding studies using RT mutants suggested that the epitope is loc ated to amino acids 652-663 of the beta' sequence. One of the MAbs which in hibited the polymerase activity of RT also mediated a dose dependent inhibi tion of the RNAP activity. (C) 2000 Federation of European Biochemical Soci eties, Published by Elsevier Science B.V. All rights reserved.