{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T01:10:42Z","timestamp":1790471442842,"version":"4.1.0"},"reference-count":54,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2012,7,1]],"date-time":"2012-07-01T00:00:00Z","timestamp":1341100800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Eukaryot Cell"],"published-print":{"date-parts":[[2012,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Est1 and Ebs1 in\n            <jats:named-content content-type=\"genus-species\">Saccharomyces cerevisiae<\/jats:named-content>\n            are paralogous proteins that arose through whole-genome duplication and that serve distinct functions in telomere maintenance and translational regulation. Here we present our functional analysis of the sole Est1\/Ebs1 homologue in the related budding yeast\n            <jats:named-content content-type=\"genus-species\">Kluyveromyces lactis<\/jats:named-content>\n            (named\n            <jats:italic>Kl<\/jats:italic>\n            Est1). We show that similar to other Est1s,\n            <jats:italic>Kl<\/jats:italic>\n            Est1 is required for normal telomere maintenance\n            <jats:italic>in vivo<\/jats:italic>\n            and full telomerase primer extension activity\n            <jats:italic>in vitro<\/jats:italic>\n            .\n            <jats:italic>Kl<\/jats:italic>\n            Est1 also associates with telomerase RNA (Ter1) and an active telomerase complex in cell extracts. Both the telomere maintenance and the Ter1 association functions of\n            <jats:italic>Kl<\/jats:italic>\n            Est1 require its N-terminal domain but not its C terminus. Analysis of clusters of point mutations revealed residues in both the N-terminal TPR subdomain and the downstream helical subdomain (DSH) that are important for telomere maintenance and Ter1 association. A UV cross-linking assay was used to establish a direct physical interaction between\n            <jats:italic>Kl<\/jats:italic>\n            Est1 and a putative stem-loop in Ter1, which also requires both the TPR and DSH subdomains. Moreover, similar to\n            <jats:named-content content-type=\"genus-species\">S. cerevisiae<\/jats:named-content>\n            Ebs1 (\n            <jats:italic>Sc<\/jats:italic>\n            Ebs1) (but not\n            <jats:italic>Sc<\/jats:italic>\n            Est1),\n            <jats:italic>Kl<\/jats:italic>\n            Est1 confers rapamycin sensitivity and may be involved in nonsense-mediated decay. Interestingly, unlike telomere regulation, this apparently separate function of\n            <jats:italic>Kl<\/jats:italic>\n            Est1 requires its C-terminal domain. Our findings provide insights on the mechanisms and evolution of Est1\/Ebs1 homologues in budding yeast and present an attractive model system for analyzing members of this multifunctional protein family.\n          <\/jats:p>","DOI":"10.1128\/ec.05319-11","type":"journal-article","created":{"date-parts":[[2012,4,29]],"date-time":"2012-04-29T00:14:56Z","timestamp":1335658496000},"page":"932-942","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":4,"title":["Functional Analysis of the Single Est1\/Ebs1 Homologue in Kluyveromyces lactis Reveals Roles in both Telomere Maintenance and Rapamycin Resistance"],"prefix":"10.1128","volume":"11","author":[{"given":"Min","family":"Hsu","sequence":"first","affiliation":[{"name":"Department of Microbiology &amp; Immunology, W. R. Hearst Microbiology Research Center, Weill Medical College of Cornell University, New York, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eun Young","family":"Yu","sequence":"additional","affiliation":[{"name":"Department of Microbiology &amp; Immunology, W. R. Hearst Microbiology Research Center, Weill Medical College of Cornell University, New York, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ondrej","family":"Spru\u0161ansk\u00fd","sequence":"additional","affiliation":[{"name":"Department of Genetics, University of Georgia, Athens, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael J.","family":"McEachern","sequence":"additional","affiliation":[{"name":"Department of Genetics, University of Georgia, Athens, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neal F.","family":"Lue","sequence":"additional","affiliation":[{"name":"Department of Microbiology &amp; Immunology, W. R. 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