title: CST for the grand finale of telomere replication.
abstract: Telomeric DNA at eukaryotic chromosome ends terminates with single stranded 3' G-rich overhangs. The overhang is generated by the interplay of several dynamic processes including semiconservative DNA replication, 3' end elongation by telomerase, C-strand fill-in synthesis and nucleolytic processing. The mammalian CST (CTC1-STN1-TEN1) complex is directly involved at several stages of telomere end formation. Elucidation of its structural organization and identification of interaction partners support the notion that mammalian CST is, as its yeast counterpart, a RPA-like complex. CST binding at mammalian telomere 3' overhangs increases upon their elongation by telomerase. Formation of a trimeric CST complex at telomeric 3'overhangs leads to telomerase inhibition and at the same time mediates a physical interaction with DNA polymerase-α. Thus CST seems to play critical roles in coordinating telomerase elongation and fill-in synthesis to complete telomere replication.
authors.affiliation: Swiss Institute for Experimental Cancer Research (ISREC); School of Life Sciences; Frontiers in Genetics National Center of Competence in Research; Ecole Polytechnique Fédérale de Lausanne (EPFL); Lausanne, Switzerland.
authors.forename: Liuh-Yow
authors.initials: LY
authors.lastname: Chen
authors.forename: Joachim
authors.initials: J
authors.lastname: Lingner
mesh_terms: D006801:Humans; D016615:Telomere / Q000378:metabolism*; D034501:Telomere-Binding Proteins / Q000378:metabolism*
chemical_list: C544945:Ctc1 protein, human; C544946:Stn1 protein, human; D034501:Telomere-Binding Proteins; C544947:Ten1 protein, human
keywords: CST; DNA polymerase-α; replication; telomerase; telomere