title: Minishelterins separate telomere length regulation and end protection in fission yeast.
abstract: The conserved shelterin complex is critical for chromosome capping and maintaining telomere length homeostasis. In fission yeast, shelterin is comprised of five proteins. Taz1, Rap1, and Poz1 function as negative regulators of telomere elongation, whereas Pot1 and Tpz1 are critical for end capping and telomerase recruitment. How the five proteins work together to safeguard chromosome ends and promote telomere length homeostasis is a matter of great interest. Using a combination of deletions, fusions, and tethers, we define key elements of shelterin important for telomere length regulation. Surprisingly, deletion of the entire Rap1 and Poz1 proteins does not impair telomere length regulation as long as a static bridge is provided between Taz1 and Tpz1. Cells harboring minishelterin display wild-type telomere length and intact subtelomeric silencing. However, protection against end fusions in G1 is compromised in the absence of Rap1. Our data reveal a remarkable plasticity in shelterin architecture and separate functions in length regulation and end protection.
authors.affiliation: Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA; Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA;
authors.forename: Lili
authors.initials: L
authors.lastname: Pan
authors.affiliation: Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA;
authors.forename: Katie
authors.initials: K
authors.lastname: Hildebrand
authors.affiliation: Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland;
authors.forename: Cian
authors.initials: C
authors.lastname: Stutz
authors.affiliation: Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland;
authors.forename: Nicolas
authors.initials: N
authors.lastname: Thomä
authors.affiliation: Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA; Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA; Howard Hughes Medical Institute, Kansas City, Missouri 64110, USA.
authors.forename: Peter
authors.initials: P
authors.lastname: Baumann
mesh_terms: D011485:Protein Binding; D012568:Schizosaccharomyces / Q000235:genetics* / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion; D019098:Telomerase / Q000378:metabolism; D016615:Telomere / Q000235:genetics* / Q000378:metabolism; D059505:Telomere Homeostasis / Q000502:physiology*; D034501:Telomere-Binding Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D029702:Schizosaccharomyces pombe Proteins; D034501:Telomere-Binding Proteins; D019098:Telomerase
keywords: end protection; fission yeast; shelterin; telomerase; telomere; telomere length regulation