Deletions near the N-terminus of HIV-1 Rev reduce RNA binding affinity and dominantly interfere with Rev function irrespective of the RNA target

Deletions near the N-terminus of HIV-1 Rev reduce RNA binding affinity and dominantly interfere... The contributions of the near N-terminal residues of Rev protein of HIV were investigated by analyzing N-terminal deletions of Rev in the context of a Rev/MS-C fusion protein that can bind and activate both the Rev responsive element (RRE) and the MS2 phage translational operator RNAs. Rev/MS-C fusion proteins deleted for residues 3–19 of Rev retained trans -activation potential for both RRE and MS2 targets. Coincidentally, peptides spanning residues 17–87 or 22–85 were functionally competent for trans -activation of RRE containing HIV-1 gag mRNA. Deletion of residues 18–24 of Rev in the Rev/MS-C fusion protein abolished the activation potential for both RRE and MS2 targets, although this mutant was competent for specific RNA binding, protein multimerization, and nuclear and nucleolar localization. Four mutants dominantly interfering with Rev activation of RRE were mapped near the N-terminus of Rev; (i) between residues 18 and 24, (ii) 25–34, (iii) 43–50, and (iv) 51–60. Of these, the mutant lacking residues 18–24 was a novel trans -dominant inhibitor of Rev and Rev/MS-C for activation of RRE or MS2 RNA, while the oligomerization domain mutants mapping between residues 25–34 or 51–60 inhibited the activation of RRE rather than MS2 RNA. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Deletions near the N-terminus of HIV-1 Rev reduce RNA binding affinity and dominantly interfere with Rev function irrespective of the RNA target

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Publisher
Springer Journals
Copyright
Copyright © 2000 by Springer-Verlag/Wien
Subject
Legacy
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s007050070001
Publisher site
See Article on Publisher Site

Abstract

The contributions of the near N-terminal residues of Rev protein of HIV were investigated by analyzing N-terminal deletions of Rev in the context of a Rev/MS-C fusion protein that can bind and activate both the Rev responsive element (RRE) and the MS2 phage translational operator RNAs. Rev/MS-C fusion proteins deleted for residues 3–19 of Rev retained trans -activation potential for both RRE and MS2 targets. Coincidentally, peptides spanning residues 17–87 or 22–85 were functionally competent for trans -activation of RRE containing HIV-1 gag mRNA. Deletion of residues 18–24 of Rev in the Rev/MS-C fusion protein abolished the activation potential for both RRE and MS2 targets, although this mutant was competent for specific RNA binding, protein multimerization, and nuclear and nucleolar localization. Four mutants dominantly interfering with Rev activation of RRE were mapped near the N-terminus of Rev; (i) between residues 18 and 24, (ii) 25–34, (iii) 43–50, and (iv) 51–60. Of these, the mutant lacking residues 18–24 was a novel trans -dominant inhibitor of Rev and Rev/MS-C for activation of RRE or MS2 RNA, while the oligomerization domain mutants mapping between residues 25–34 or 51–60 inhibited the activation of RRE rather than MS2 RNA.

Journal

Archives of VirologySpringer Journals

Published: Dec 1, 2000

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