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Institutes of Health","award":["RO1 AI150493"],"award-info":[{"award-number":["RO1 AI150493"]}]},{"name":"National Institutes of Health","award":["U54 AI150472"],"award-info":[{"award-number":["U54 AI150472"]}]},{"name":"National Institutes of Health","award":["P30 GM124169"],"award-info":[{"award-number":["P30 GM124169"]}]},{"name":"National Institutes of Health","award":["S10OD018483"],"award-info":[{"award-number":["S10OD018483"]}]},{"name":"National Institutes of Health","award":["DMR-1829070"],"award-info":[{"award-number":["DMR-1829070"]}]},{"name":"National Institutes of Health","award":["GM-124166"],"award-info":[{"award-number":["GM-124166"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>Interactions between lysyl\u2013tRNA synthetase (LysRS) and HIV-1 Gag facilitate selective packaging of the HIV-1 reverse transcription primer, tRNALys3. During HIV-1 infection, LysRS is phosphorylated at S207, released from a multi-aminoacyl\u2013tRNA synthetase complex and packaged into progeny virions. LysRS is critical for proper targeting of tRNALys3 to the primer-binding site (PBS) by specifically binding a PBS-adjacent tRNA-like element (TLE), which promotes release of the tRNA proximal to the PBS. However, whether LysRS phosphorylation plays a role in this process remains unknown. Here, we used a combination of binding assays, RNA chemical probing, and small-angle X-ray scattering to show that both wild-type (WT) and a phosphomimetic S207D LysRS mutant bind similarly to the HIV-1 genomic RNA (gRNA) 5\u2032UTR via direct interactions with the TLE and stem loop 1 (SL1) and have a modest preference for binding dimeric gRNA. Unlike WT, S207D LysRS bound in an open conformation and increased the dynamics of both the PBS region and SL1. A new working model is proposed wherein a dimeric phosphorylated LysRS\/tRNA complex binds to a gRNA dimer to facilitate tRNA primer release and placement onto the PBS. Future anti-viral strategies that prevent this host factor-gRNA interaction are envisioned.<\/jats:p>","DOI":"10.3390\/v14071556","type":"journal-article","created":{"date-parts":[[2022,7,18]],"date-time":"2022-07-18T01:53:22Z","timestamp":1658109202000},"page":"1556","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Phosphomimetic S207D Lysyl\u2013tRNA Synthetase Binds HIV-1 5\u2032UTR in an Open Conformation and Increases RNA Dynamics"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3214-7635","authenticated-orcid":false,"given":"William A.","family":"Cantara","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for Retrovirus Research, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1527-0882","authenticated-orcid":false,"given":"Chathuri","family":"Pathirage","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for Retrovirus Research, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joshua","family":"Hatterschide","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for Retrovirus Research, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erik D.","family":"Olson","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for Retrovirus Research, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin","family":"Musier-Forsyth","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for Retrovirus Research, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA"},{"name":"Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,7,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3246","DOI":"10.1128\/jvi.67.6.3246-3253.1993","article-title":"Identification of tRNAs incorporated into wild-type and mutant human immunodeficiency virus type 1","volume":"67","author":"Jiang","year":"1993","journal-title":"J. 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