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However, the mechanism by which \u03a8 promotes selective packaging of the gRNA is not well understood. We used fluorescence correlation spectroscopy and quenching data to monitor the binding of recombinant HIV-1 Gag protein to Cy5-tagged 190-base RNAs. At physiological ionic strength, Gag binds with very similar, nanomolar affinities to both \u03a8-containing and control RNAs. We challenged these interactions by adding excess competing tRNA; introducing mutations in Gag; or raising the ionic strength. These modifications all revealed high specificity for \u03a8. This specificity is evidently obscured in physiological salt by non-specific, predominantly electrostatic interactions. This nonspecific activity was attenuated by mutations in the MA, CA, and NC domains, including CA mutations disrupting Gag-Gag interaction. We propose that gRNA is selectively packaged because binding to \u03a8 nucleates virion assembly with particular efficiency.<\/jats:p>","DOI":"10.7554\/elife.27055","type":"journal-article","created":{"date-parts":[[2017,7,20]],"date-time":"2017-07-20T08:01:53Z","timestamp":1500537713000},"source":"Crossref","is-referenced-by-count":74,"title":["Dissection of specific binding of HIV-1 Gag to the 'packaging signal' in viral RNA"],"prefix":"10.7554","volume":"6","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7733-5138","authenticated-orcid":true,"given":"Mauricio","family":"Comas-Garcia","sequence":"first","affiliation":[{"name":"HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Siddhartha AK","family":"Datta","sequence":"additional","affiliation":[{"name":"HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, 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