000114894 001__ 114894
000114894 005__ 20181203021032.0
000114894 0247_ $$2doi$$a10.1016/S0960-9822(03)00169-6
000114894 037__ $$aARTICLE
000114894 245__ $$aTelomere maintenance in fission yeast requires an Est1 ortholog
000114894 269__ $$a2003
000114894 260__ $$c2003
000114894 336__ $$aJournal Articles
000114894 500__ $$aUniversity of Colorado Health Sciences Center, 4200 East 9th Avenue, Denver, CO 80262, USA.
000114894 520__ $$aTelomerase regulation is critical to genome maintenance yet remains poorly understood. Without telomerase's ability to synthesize telomere repeats, chromosome ends shorten progressively, as conventional DNA polymerases cannot fully replicate the ends of linear molecules. In Saccharomyces cerevisiae, telomerase activity in vivo absolutely depends on a set of telomerase accessory proteins that includes Est1p, which appears to recruit or activate telomerase at the site of polymerization. Thus, est1Delta cells have the same cellular senescence phenotype as cells lacking either the catalytic protein subunit of telomerase or its template-containing RNA subunit. While the telomerase protein is highly conserved among eukaryotes, the apparent lack of Est1p homologs has frustrated efforts to describe a common mechanism of telomerase recruitment and activation. Here, we describe SpEst1p, a homolog of Est1p from the evolutionarily distant Schizosaccharomyces pombe. Like ScEst1p, SpEst1p is required for telomerase activity in vivo. Coupled with the identification of an orthologous Est1 protein in humans [10], this suggests a much wider conservation of telomerase regulation than was previously known. Strikingly, in cells with compromised telomere function (taz1Delta), SpEst1p loss confers a lethal germination phenotype, while telomerase loss does not, indicating that SpEst1p plays an unexpected additional role in chromosome end protection.
000114894 700__ $$aBeernink, H. T.
000114894 700__ $$aMiller, K.
000114894 700__ $$aDeshpande, A.
000114894 700__ $$0244404$$g113607$$aBucher, P.
000114894 700__ $$aCooper, J. P.
000114894 773__ $$j13$$tCurr Biol$$k7$$q575-80
000114894 909C0 $$xU11780$$0252244$$pGR-BUCHER
000114894 909CO $$pSV$$particle$$ooai:infoscience.tind.io:114894
000114894 937__ $$aGR-BUCHER-ARTICLE-2003-002
000114894 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000114894 980__ $$aARTICLE