Article abstract
Nature Structural & Molecular Biology 15, 990 - 997 (2008)
Published online: 24 August 2008 | doi:10.1038/nsmb.1472
The Est3 protein associates with yeast telomerase through an OB-fold domain
Jaesung Lee1,3, Edward K Mandell1,2,3, Timothy M Tucey1, Danna K Morris2 & Victoria Lundblad1
Abstract
The Ever shorter telomeres 3 (Est3) protein is a small regulatory subunit of yeast telomerase which is dispensable for enzyme catalysis but essential for telomere replication in vivo. Using structure prediction combined with in vivo characterization, we show here that Est3 consists of a predicted OB (oligosaccharide/oligonucleotide binding)-fold. We used mutagenesis of predicted surface residues to generate a functional map of one surface of Est3, identifying a site that mediates association with the telomerase complex. Unexpectedly, the predicted OB-fold of Est3 is structurally similar to the OB-fold of the human TPP1 protein, despite the fact that Est3 and TPP1, as components of telomerase and a telomere-capping complex, respectively, perform functionally distinct tasks at chromosome ends. Our analysis of Est3 may be instructive in generating comparable missense mutations on the surface of the OB-fold domain of TPP1.
- The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.
- Graduate Program in Cell and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
- These authors contributed equally to this work.
Correspondence to: Victoria Lundblad1 e-mail: lundblad@salk.edu
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