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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2017,7,11]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>Ribonucleases are molecular scissors that catalyze the cleavage of RNA phosphodiester bonds and play essential roles in RNA processing and maturation. Precursor ribosomal RNA (rRNA) must be processed by several ribonucleases, including the endonuclease Las1, in a carefully orchestrated manner to generate the mature ribosomal subunits. Las1 is essential for cell viability, and mutations in the mammalian gene have been linked with human disease, underscoring the importance of this enzyme. Here, we show that, on its own, Las1 has weak activity; however, when associated with its binding partner, the polynucleotide kinase Grc3, Las1 is programmed to efficiently cleave pre-rRNA at the C2 site. Together, Grc3 and Las1 assemble into a higher-order complex exquisitely primed for cleavage and phosphorylation of RNA.<\/jats:p>","DOI":"10.1073\/pnas.1703133114","type":"journal-article","created":{"date-parts":[[2017,6,26]],"date-time":"2017-06-26T20:40:30Z","timestamp":1498509630000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":47,"title":["Grc3 programs the essential endoribonuclease Las1 for specific RNA cleavage"],"prefix":"10.1073","volume":"114","author":[{"given":"Monica C.","family":"Pillon","sequence":"first","affiliation":[{"name":"Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mack","family":"Sobhany","sequence":"additional","affiliation":[{"name":"Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mario J.","family":"Borgnia","sequence":"additional","affiliation":[{"name":"Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jason G.","family":"Williams","sequence":"additional","affiliation":[{"name":"Epigenetics and Stem Cell Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2106-3102","authenticated-orcid":false,"given":"Robin E.","family":"Stanley","sequence":"additional","affiliation":[{"name":"Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2017,6,26]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583510000181","article-title":"Nucleases: Diversity of structure, function and mechanism","volume":"44","author":"Yang W","year":"2011","unstructured":"W Yang, Nucleases: Diversity of structure, function and mechanism. 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