Open Access
Structure, volume 20, issue 1, pages 28-39
Telomerase and Telomere-Associated Proteins: Structural Insights into Mechanism and Evolution
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Department of Chemistry and Biochemistry, University of Colorado, Boulder, Boulder, CO 80309, USA
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Publication type: Journal Article
Publication date: 2012-01-11
PubMed ID:
22244753
Molecular Biology
Structural Biology
Abstract
Recent advances in our structural understanding of telomerase and telomere-associated proteins have contributed significantly to elucidating the molecular mechanisms of telomere maintenance. The structures of telomerase TERT domains have provided valuable insights into how experimentally identified conserved motifs contribute to the telomerase reverse transcriptase reaction. Additionally, structures of telomere-associated proteins in a variety of organisms have revealed that, across evolution, telomere-maintenance mechanisms employ common structural elements. For example, the single-stranded 3' overhang of telomeric DNA is specifically and tightly bound by an OB-fold in nearly all species, including ciliates (TEBP and Pot1a), fission yeast (SpPot1), budding yeast (Cdc13), and humans (hPOT1). Structures of the yeast Cdc13, Stn1, and Ten1 proteins demonstrated that telomere maintenance is regulated by a complex that bears significant similarity to the RPA heterotrimer. Similarly, proteins that specifically bind double-stranded telomeric DNA in divergent species use homeodomains to execute their functions (human TRF1 and TRF2 and budding yeast ScRap1). Likewise, the conserved protein Rap1, which is found in budding yeast, fission yeast, and humans, contains a structural motif that is known to be critical for protein-protein interaction. In addition to revealing the common underlying themes of telomere maintenance, structures have also elucidated the specific mechanisms by which many of these proteins function, including identifying a telomere-specific domain in Stn1 and how the human TRF proteins avoid heterodimerization. In this review, we summarize the high-resolution structures of telomerase and telomere-associated proteins and discuss the emergent common structural themes among these proteins. We also address how these high-resolution structures complement biochemical and cellular studies to enhance our understanding of telomere maintenance and function.
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- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Lewis K. A., Wuttke D. S. Telomerase and Telomere-Associated Proteins: Structural Insights into Mechanism and Evolution // Structure. 2012. Vol. 20. No. 1. pp. 28-39.
GOST all authors (up to 50)
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Lewis K. A., Wuttke D. S. Telomerase and Telomere-Associated Proteins: Structural Insights into Mechanism and Evolution // Structure. 2012. Vol. 20. No. 1. pp. 28-39.
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TY - JOUR
DO - 10.1016/j.str.2011.10.017
UR - https://doi.org/10.1016%2Fj.str.2011.10.017
TI - Telomerase and Telomere-Associated Proteins: Structural Insights into Mechanism and Evolution
T2 - Structure
AU - Lewis, Karen A
AU - Wuttke, Deborah S.
PY - 2012
DA - 2012/01/11 00:00:00
PB - Elsevier
SP - 28-39
IS - 1
VL - 20
PMID - 22244753
SN - 0969-2126
SN - 1878-4186
ER -
Cite this
BibTex
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@article{2012_Lewis,
author = {Karen A Lewis and Deborah S. Wuttke},
title = {Telomerase and Telomere-Associated Proteins: Structural Insights into Mechanism and Evolution},
journal = {Structure},
year = {2012},
volume = {20},
publisher = {Elsevier},
month = {jan},
url = {https://doi.org/10.1016%2Fj.str.2011.10.017},
number = {1},
pages = {28--39},
doi = {10.1016/j.str.2011.10.017}
}
Cite this
MLA
Copy
Lewis, Karen A., and Deborah S. Wuttke. “Telomerase and Telomere-Associated Proteins: Structural Insights into Mechanism and Evolution.” Structure, vol. 20, no. 1, Jan. 2012, pp. 28-39. https://doi.org/10.1016%2Fj.str.2011.10.017.