Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Sensitive in vitro analysis of HIV-1 Rev multimerization.

P C Brice1, A C Kelley, P J Butler

  • 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. pjgb@mrc-lmb.cam.ac.uk

Nucleic Acids Research
|April 29, 1999
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The roller coaster flight strategy of bar-headed geese conserves energy during Himalayan migrations.

Science (New York, N.Y.)·2015
Same author

An increase in minimum metabolic rate and not activity explains field metabolic rate changes in a breeding seabird.

The Journal of experimental biology·2013
Same author

The paradox of extreme high-altitude migration in bar-headed geese Anser indicus.

Proceedings. Biological sciences·2012
Same author

Population growth, the dependency rate, and the pace of economic development.

Population studies·2011
Same author

Assessing the validity of the accelerometry technique for estimating the energy expenditure of diving double-crested cormorants Phalacrocorax auritus.

Physiological and biochemical zoology : PBZ·2011
Same author

Spatial dynamics of bar-headed geese migration in the context of H5N1.

Journal of the Royal Society, Interface·2010
Same journal

VeloRM: disentangling pre- and post-splicing RNA modification dynamics at single-cell resolution.

Nucleic acids research·2026
Same journal

Accessibility of telomeric overhangs to stabilizing small-molecule ligands.

Nucleic acids research·2026
Same journal

Multivalent interactions mediate SNAIL transcription factor stimulation of the nucleosome deacetylase activity of the CoREST complex.

Nucleic acids research·2026
Same journal

Genome-wide mapping of DNA G-quadruplexes in Trypanosoma brucei chromatin reveals enrichment in coding regions and transcription start sites.

Nucleic acids research·2026
Same journal

Epigenetic landscape of synthetic human centromere core regions: CENP-A assembly and euchromatic modifications interdependently antagonize heterochromatin accumulation.

Nucleic acids research·2026
Same journal

MAPK/ERK signaling regulates H3K9me3 heterochromatin reorganization to confer mesendoderm developmental competence.

Nucleic acids research·2026
See all related articles

Rev protein oligomerization is crucial for HIV-1 mRNA export. Re-examination shows M7 mutant oligomerizes on RNA, contrary to prior studies, making it unsuitable for multimerization research.

Area of Science:

  • Molecular Biology
  • Virology
  • Structural Biology

Background:

  • The Rev protein of human immunodeficiency virus type 1 (HIV-1) is essential for nuclear export of unspliced viral mRNAs.
  • Rev oligomerization on the Rev response element (RRE) is critical for its function.
  • Previous studies identified two oligomerization sites and characterized mutants M4 and M7, which bind RNA but were reported to lack oligomerization.

Purpose of the Study:

  • To re-examine the in vitro oligomerization of Rev mutants M4 and M7 on Rev response elements.
  • To clarify the role of these mutants in Rev multimerization studies.
  • To validate the suitability of M7 as a paradigm for Rev multimerization.

Main Methods:

  • In vitro binding assays using model Rev response elements.

Related Experiment Videos

  • Improved gel mobility shift assays to analyze protein-RNA interactions and oligomerization.
  • Comparison of wild-type Rev protein with M4 and M7 mutants.

    • Main Results:

    • Both M4 and M7 mutants form oligomers on the Rev response element in vitro.
    • Mutants exhibit slightly lower RNA binding affinities compared to wild-type Rev.
    • M7 shows reduced specific affinity but retains significant oligomerization capability post-binding.
    • M4 demonstrates a deficiency in multimerization, consistent with previous findings.

    Conclusions:

    • The previously defined oligomerization sites in Rev are correctly identified.
    • The M7 deletion mutant is inappropriate for studying Rev oligomerization due to its retained multimerization capacity.
    • Re-evaluation of Rev mutants is crucial for accurate understanding of viral protein function and multimerization mechanisms.