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Journal of Biological Chemistry, volume 286, issue 30, pages 26431-26439

Stimulation of Yeast Telomerase Activity by the Ever Shorter Telomere 3 (Est3) Subunit Is Dependent on Direct Interaction with the Catalytic Protein Est2

Talley Jennell M 1
Dezwaan Diane C 2
Maness Leslie D 3
Freeman Brian C. 2
Friedman Katherine 3
1
 
Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235 USA.
2
 
Department of Cell and Developmental Biology, University of Illinois at Urbana‐Champaign, Urbana, Illinois 61801
3
 
*Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235
Publication typeJournal Article
Publication date2011-07-01
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor4.8
ISSN00219258, 1083351X
Biochemistry
Molecular Biology
Cell Biology
Abstract
Telomerase is a multisubunit enzyme that maintains genome stability through its role in telomere replication. Although the Est3 protein is long recognized as an essential telomerase component, how it associates with and functions in the telomerase complex has remained enigmatic. Here we provide the first evidence of a direct interaction between Saccharomyces cerevisiae Est3p and the catalytic protein subunit (Est2p) by demonstrating that recombinant Est3p binds the purified telomerase essential N-terminal (TEN) domain of Est2p in vitro. Mutations in a small cluster of amino acids predicted to lie on the surface of Est3p disrupt this interaction with Est2p, reduce assembly of Est3p with telomerase in vivo, and cause telomere shortening and senescence. We also show that recombinant Est3p stimulates telomerase activity above basal levels in vitro in a manner dependent on the Est2p TEN domain interaction. Together, these results define a direct binding interaction between Est3p and Est2p and reconcile the effect of S. cerevisiae Est3p with previous experiments showing that Est3p homologs in related yeast species influence telomerase activity. Additionally, it contributes functional support to the idea that Est3p is structurally related to the mammalian shelterin protein, TPP1, which also influences telomerase activity through interaction with the Est2p homolog, TERT.

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GOST Copy
Talley J. M. et al. Stimulation of Yeast Telomerase Activity by the Ever Shorter Telomere 3 (Est3) Subunit Is Dependent on Direct Interaction with the Catalytic Protein Est2 // Journal of Biological Chemistry. 2011. Vol. 286. No. 30. pp. 26431-26439.
GOST all authors (up to 50) Copy
Talley J. M., Dezwaan D. C., Maness L. D., Freeman B. C., Friedman K. Stimulation of Yeast Telomerase Activity by the Ever Shorter Telomere 3 (Est3) Subunit Is Dependent on Direct Interaction with the Catalytic Protein Est2 // Journal of Biological Chemistry. 2011. Vol. 286. No. 30. pp. 26431-26439.
RIS |
Cite this
RIS Copy
TY - JOUR
DO - 10.1074/jbc.M111.228635
UR - https://doi.org/10.1074%2Fjbc.M111.228635
TI - Stimulation of Yeast Telomerase Activity by the Ever Shorter Telomere 3 (Est3) Subunit Is Dependent on Direct Interaction with the Catalytic Protein Est2
T2 - Journal of Biological Chemistry
AU - Talley, Jennell M
AU - Dezwaan, Diane C
AU - Maness, Leslie D
AU - Freeman, Brian C.
AU - Friedman, Katherine
PY - 2011
DA - 2011/07/01 00:00:00
PB - American Society for Biochemistry and Molecular Biology
SP - 26431-26439
IS - 30
VL - 286
PMID - 21659533
SN - 0021-9258
SN - 1083-351X
ER -
BibTex |
Cite this
BibTex Copy
@article{2011_Talley,
author = {Jennell M Talley and Diane C Dezwaan and Leslie D Maness and Brian C. Freeman and Katherine Friedman},
title = {Stimulation of Yeast Telomerase Activity by the Ever Shorter Telomere 3 (Est3) Subunit Is Dependent on Direct Interaction with the Catalytic Protein Est2},
journal = {Journal of Biological Chemistry},
year = {2011},
volume = {286},
publisher = {American Society for Biochemistry and Molecular Biology},
month = {jul},
url = {https://doi.org/10.1074%2Fjbc.M111.228635},
number = {30},
pages = {26431--26439},
doi = {10.1074/jbc.M111.228635}
}
MLA
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MLA Copy
Talley, Jennell M., et al. “Stimulation of Yeast Telomerase Activity by the Ever Shorter Telomere 3 (Est3) Subunit Is Dependent on Direct Interaction with the Catalytic Protein Est2.” Journal of Biological Chemistry, vol. 286, no. 30, Jul. 2011, pp. 26431-26439. https://doi.org/10.1074%2Fjbc.M111.228635.
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