Open Access
Proceedings of the National Academy of Sciences of the United States of America, volume 111, issue 1, pages 214-218
Structure of Est3 reveals a bimodal surface with differential roles in telomere replication
Rao Timsi
1
,
Lubin Johnathan W
2
,
Armstrong Geoffrey S.
1
,
Tucey Timothy M
2, 3
,
Lundblad Victoria
2
,
Wuttke Deborah S
1
1
Department of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO 80309-0596;
|
2
Salk Institute for Biological Sciences, La Jolla, CA 92037-1099; and
|
3
Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093-0130
|
Publication type: Journal Article
Publication date: 2013-12-16
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 11.1
ISSN: 00278424, 10916490
PubMed ID:
24344315
Multidisciplinary
Abstract
Significance Despite the central role that budding yeast has played in telomere biology, structural analysis of the subunits of the yeast telomerase complex has proven to be challenging. We present here the structure of a yeast telomerase protein, Est3, using the resolution-adapted structural recombination Rosetta strategy that combines NMR experimental data with database-derived conformational sampling. A comprehensive in vivo analysis of the experimentally determined Est3 protein surface has identified two functionally important surfaces, opening up the possibility of a similar discovery in the structurally similar human TPP1 protein. Telomerase is essential for continuous cellular proliferation. Substantial insights have come from studies of budding yeast telomerase, which consists of a catalytic core in association with two regulatory proteins, ever shorter telomeres 1 and 3 (Est1 and Est3). We report here a high-resolution structure of the Est3 telomerase subunit determined using a recently developed strategy that combines minimal NMR experimental data with Rosetta de novo structure prediction algorithms. Est3 adopts an overall protein fold which is structurally similar to that adopted by the shelterin component TPP1. However, the characteristics of the surface of the experimentally determined Est3 structure are substantially different from those predicted by prior homology-based models of Est3. Structure-guided mutagenesis of the complete surface of the Est3 protein reveals two adjacent patches on a noncanonical face of the protein that differentially mediate telomere function. Mapping these two patches on the Est3 structure defines a set of shared features between Est3 and HsTPP1, suggesting an analogous multifunctional surface on TPP1.
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Rao T. et al. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication // Proceedings of the National Academy of Sciences of the United States of America. 2013. Vol. 111. No. 1. pp. 214-218.
GOST all authors (up to 50)
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Rao T., Lubin J. W., Armstrong G. S., Tucey T. M., Lundblad V., Wuttke D. S. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication // Proceedings of the National Academy of Sciences of the United States of America. 2013. Vol. 111. No. 1. pp. 214-218.
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RIS
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TY - JOUR
DO - 10.1073/pnas.1316453111
UR - https://doi.org/10.1073%2Fpnas.1316453111
TI - Structure of Est3 reveals a bimodal surface with differential roles in telomere replication
T2 - Proceedings of the National Academy of Sciences of the United States of America
AU - Rao, Timsi
AU - Lubin, Johnathan W
AU - Armstrong, Geoffrey S.
AU - Tucey, Timothy M
AU - Lundblad, Victoria
AU - Wuttke, Deborah S
PY - 2013
DA - 2013/12/16 00:00:00
PB - Proceedings of the National Academy of Sciences (PNAS)
SP - 214-218
IS - 1
VL - 111
PMID - 24344315
SN - 0027-8424
SN - 1091-6490
ER -
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@article{2013_Rao,
author = {Timsi Rao and Johnathan W Lubin and Geoffrey S. Armstrong and Timothy M Tucey and Victoria Lundblad and Deborah S Wuttke},
title = {Structure of Est3 reveals a bimodal surface with differential roles in telomere replication},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {2013},
volume = {111},
publisher = {Proceedings of the National Academy of Sciences (PNAS)},
month = {dec},
url = {https://doi.org/10.1073%2Fpnas.1316453111},
number = {1},
pages = {214--218},
doi = {10.1073/pnas.1316453111}
}
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MLA
Copy
Rao, Timsi, et al. “Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.” Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 1, Dec. 2013, pp. 214-218. https://doi.org/10.1073%2Fpnas.1316453111.