<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>76(16)</volume><submitter>Attrill HL</submitter><pubmed_abstract>The US11 protein of herpes simplex virus type 1 (HSV-1) is a small, highly basic phosphoprotein expressed at late times during infection. US11 localizes to the nucleolus in infected cells, can associate with ribosomes, and has been shown to bind RNA. The RNA substrates of US11 identified thus far have no apparent role in the virus lytic cycle, so we set out to identify a novel, biologically relevant RNA substrate(s) for this protein in HSV-1-infected cells. We designed a reverse transcriptase PCR-based protocol that allowed specific selection of a 600-bp RNA binding partner for US11. This RNA sequence, designated 12/14, is present in the coterminal HSV-1 mRNAs UL12, UL13, and UL14. We show that the binding of US11 to 12/14 is sequence-specific and mediated by the C-terminal domain of the p</pubmed_abstract><journal>Journal of virology</journal><pagination>8090-100</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC155164</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The herpes simplex virus type 1 US11 protein binds the coterminal UL12, UL13, and UL14 RNAs and regulates UL13 expression in vivo.</pubmed_title><pmcid>PMC155164</pmcid><pubmed_authors>Clements JB</pubmed_authors><pubmed_authors>Attrill HL</pubmed_authors><pubmed_authors>Graham SV</pubmed_authors><pubmed_authors>Cumming SA</pubmed_authors></additional><is_claimable>false</is_claimable><name>The herpes simplex virus type 1 US11 protein binds the coterminal UL12, UL13, and UL14 RNAs and regulates UL13 expression in vivo.</name><description>The US11 protein of herpes simplex virus type 1 (HSV-1) is a small, highly basic phosphoprotein expressed at late times during infection. US11 localizes to the nucleolus in infected cells, can associate with ribosomes, and has been shown to bind RNA. The RNA substrates of US11 identified thus far have no apparent role in the virus lytic cycle, so we set out to identify a novel, biologically relevant RNA substrate(s) for this protein in HSV-1-infected cells. We designed a reverse transcriptase PCR-based protocol that allowed specific selection of a 600-bp RNA binding partner for US11. This RNA sequence, designated 12/14, is present in the coterminal HSV-1 mRNAs UL12, UL13, and UL14. We show that the binding of US11 to 12/14 is sequence-specific and mediated by the C-terminal domain of the p</description><dates><release>2002-01-01T00:00:00Z</release><publication>2002 Aug</publication><modification>2025-04-05T15:32:09.767Z</modification><creation>2019-06-05T19:16:10Z</creation></dates><accession>S-EPMC155164</accession><cross_references><pubmed>12134014</pubmed><doi>10.1128/jvi.76.16.8090-8100.2002</doi></cross_references></HashMap>