Open Access
Open access
Molecular Biology of the Cell, volume 14, issue 1, pages 1-13

N-terminal Domain of Yeast Telomerase Reverse Transcriptase: Recruitment of Est3p to the Telomerase Complex

Friedman Katherine L. 1
Heit Jeremy J. 2
LONG DAVID M. 3
Cech Thomas R 2
1
 
Vanderbilt University, Department of Biological Sciences, Nashville, Tennessee 37235;
2
 
Department of Chemistry and Biochemistry and Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado 80309-0215; and
3
 
Department of Plant Sciences, Montana State University, Bozeman, Montana 59717
Publication typeJournal Article
Publication date2003-01-16
Quartile SCImago
Q1
Quartile WOS
Q3
Impact factor3.3
ISSN10591524, 19394586
Molecular Biology
Cell Biology
Abstract

Telomerase is a reverse transcriptase that maintains chromosome ends. The N-terminal half of the catalytic protein subunit (TERT) contains three functional domains (I, II, and III) that are conserved among TERTs but not found in other reverse transcriptases. Guided by an amino acid sequence alignment of nine TERT proteins, mutations were introduced into yeast TERT (Est2p). In support of the proposed alignment, mutation of virtually all conserved residues resulted in loss-of-function or temperature sensitivity, accompanied by telomere shortening. Overexpression of telomerase component Est3p led to allele-specific suppression of the temperature-sensitive mutations in region I, suggesting that Est3p interacts with this protein domain. As predicted by the genetic results, a lethal mutation in region I resulted in loss of Est3p from the telomerase complex. We conclude that Est2p region I is required for the recruitment of Est3p to yeast telomerase. Given the phylogenetic conservation of region I of TERT, this protein domain may provide the equivalent function in all telomerases.

Citations by journals

1
2
3
4
5
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 5, 8.47%
Nature Structural and Molecular Biology
5 publications, 8.47%
Molecular and Cellular Biology
Molecular and Cellular Biology, 4, 6.78%
Molecular and Cellular Biology
4 publications, 6.78%
Biochemistry (Moscow)
Biochemistry (Moscow), 3, 5.08%
Biochemistry (Moscow)
3 publications, 5.08%
PLoS ONE
PLoS ONE, 3, 5.08%
PLoS ONE
3 publications, 5.08%
Genes and Development
Genes and Development, 3, 5.08%
Genes and Development
3 publications, 5.08%
Molecular Biology of the Cell
Molecular Biology of the Cell, 3, 5.08%
Molecular Biology of the Cell
3 publications, 5.08%
Biochimie
Biochimie, 2, 3.39%
Biochimie
2 publications, 3.39%
Current Opinion in Structural Biology
Current Opinion in Structural Biology, 2, 3.39%
Current Opinion in Structural Biology
2 publications, 3.39%
Journal of Biological Chemistry
Journal of Biological Chemistry, 2, 3.39%
Journal of Biological Chemistry
2 publications, 3.39%
Biomolecular NMR Assignments
Biomolecular NMR Assignments, 1, 1.69%
Biomolecular NMR Assignments
1 publication, 1.69%
Doklady Biochemistry and Biophysics
Doklady Biochemistry and Biophysics, 1, 1.69%
Doklady Biochemistry and Biophysics
1 publication, 1.69%
Scientific Reports
Scientific Reports, 1, 1.69%
Scientific Reports
1 publication, 1.69%
FEBS Letters
FEBS Letters, 1, 1.69%
FEBS Letters
1 publication, 1.69%
Molecular Biology
Molecular Biology, 1, 1.69%
Molecular Biology
1 publication, 1.69%
Journal of Cell Science
Journal of Cell Science, 1, 1.69%
Journal of Cell Science
1 publication, 1.69%
Cell
Cell, 1, 1.69%
Cell
1 publication, 1.69%
Future Oncology
Future Oncology, 1, 1.69%
Future Oncology
1 publication, 1.69%
Biochemical Journal
Biochemical Journal, 1, 1.69%
Biochemical Journal
1 publication, 1.69%
Nature Communications
Nature Communications, 1, 1.69%
Nature Communications
1 publication, 1.69%
PLoS Genetics
PLoS Genetics, 1, 1.69%
PLoS Genetics
1 publication, 1.69%
Structure
Structure, 1, 1.69%
Structure
1 publication, 1.69%
Yeast
Yeast, 1, 1.69%
Yeast
1 publication, 1.69%
Insect Molecular Biology
Insect Molecular Biology, 1, 1.69%
Insect Molecular Biology
1 publication, 1.69%
Protein Science
Protein Science, 1, 1.69%
Protein Science
1 publication, 1.69%
Biochemistry
Biochemistry, 1, 1.69%
Biochemistry
1 publication, 1.69%
Critical Reviews in Biochemistry and Molecular Biology
Critical Reviews in Biochemistry and Molecular Biology, 1, 1.69%
Critical Reviews in Biochemistry and Molecular Biology
1 publication, 1.69%
Molecular Biology and Evolution
Molecular Biology and Evolution, 1, 1.69%
Molecular Biology and Evolution
1 publication, 1.69%
Nucleic Acids Research
Nucleic Acids Research, 1, 1.69%
Nucleic Acids Research
1 publication, 1.69%
Genetics
Genetics, 1, 1.69%
Genetics
1 publication, 1.69%
1
2
3
4
5

Citations by publishers

1
2
3
4
5
6
7
8
9
Springer Nature
Springer Nature, 9, 15.25%
Springer Nature
9 publications, 15.25%
Elsevier
Elsevier, 6, 10.17%
Elsevier
6 publications, 10.17%
Pleiades Publishing
Pleiades Publishing, 5, 8.47%
Pleiades Publishing
5 publications, 8.47%
Wiley
Wiley, 4, 6.78%
Wiley
4 publications, 6.78%
Public Library of Science (PLoS)
Public Library of Science (PLoS), 4, 6.78%
Public Library of Science (PLoS)
4 publications, 6.78%
American Society for Microbiology
American Society for Microbiology, 4, 6.78%
American Society for Microbiology
4 publications, 6.78%
Cold Spring Harbor Laboratory
Cold Spring Harbor Laboratory, 3, 5.08%
Cold Spring Harbor Laboratory
3 publications, 5.08%
American Society for Cell Biology (ASCB)
American Society for Cell Biology (ASCB), 3, 5.08%
American Society for Cell Biology (ASCB)
3 publications, 5.08%
American Society for Biochemistry and Molecular Biology
American Society for Biochemistry and Molecular Biology, 2, 3.39%
American Society for Biochemistry and Molecular Biology
2 publications, 3.39%
Oxford University Press
Oxford University Press, 2, 3.39%
Oxford University Press
2 publications, 3.39%
The Company of Biologists
The Company of Biologists, 1, 1.69%
The Company of Biologists
1 publication, 1.69%
Future Medicine
Future Medicine, 1, 1.69%
Future Medicine
1 publication, 1.69%
Portland Press
Portland Press, 1, 1.69%
Portland Press
1 publication, 1.69%
American Chemical Society (ACS)
American Chemical Society (ACS), 1, 1.69%
American Chemical Society (ACS)
1 publication, 1.69%
Taylor & Francis
Taylor & Francis, 1, 1.69%
Taylor & Francis
1 publication, 1.69%
Genetics Society of America
Genetics Society of America, 1, 1.69%
Genetics Society of America
1 publication, 1.69%
Proceedings of the National Academy of Sciences (PNAS)
Proceedings of the National Academy of Sciences (PNAS), 1, 1.69%
Proceedings of the National Academy of Sciences (PNAS)
1 publication, 1.69%
eLife Sciences Publications
eLife Sciences Publications, 1, 1.69%
eLife Sciences Publications
1 publication, 1.69%
American Society of Hematology
American Society of Hematology, 1, 1.69%
American Society of Hematology
1 publication, 1.69%
Annual Reviews
Annual Reviews, 1, 1.69%
Annual Reviews
1 publication, 1.69%
1
2
3
4
5
6
7
8
9
  • We do not take into account publications that without a DOI.
  • Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
  • Statistics recalculated weekly.
Metrics
Share
Cite this
GOST |
Cite this
GOST Copy
Friedman K. L. et al. N-terminal Domain of Yeast Telomerase Reverse Transcriptase: Recruitment of Est3p to the Telomerase Complex // Molecular Biology of the Cell. 2003. Vol. 14. No. 1. pp. 1-13.
GOST all authors (up to 50) Copy
Friedman K. L., Heit J. J., LONG D. M., Cech T. R. N-terminal Domain of Yeast Telomerase Reverse Transcriptase: Recruitment of Est3p to the Telomerase Complex // Molecular Biology of the Cell. 2003. Vol. 14. No. 1. pp. 1-13.
RIS |
Cite this
RIS Copy
TY - JOUR
DO - 10.1091/mbc.E02-06-0327
UR - https://doi.org/10.1091%2Fmbc.E02-06-0327
TI - N-terminal Domain of Yeast Telomerase Reverse Transcriptase: Recruitment of Est3p to the Telomerase Complex
T2 - Molecular Biology of the Cell
AU - Friedman, Katherine L.
AU - Heit, Jeremy J.
AU - LONG, DAVID M.
AU - Cech, Thomas R
PY - 2003
DA - 2003/01/16 00:00:00
PB - American Society for Cell Biology (ASCB)
SP - 1-13
IS - 1
VL - 14
PMID - 12529422
SN - 1059-1524
SN - 1939-4586
ER -
BibTex |
Cite this
BibTex Copy
@article{2003_Friedman,
author = {Katherine L. Friedman and Jeremy J. Heit and DAVID M. LONG and Thomas R Cech},
title = {N-terminal Domain of Yeast Telomerase Reverse Transcriptase: Recruitment of Est3p to the Telomerase Complex},
journal = {Molecular Biology of the Cell},
year = {2003},
volume = {14},
publisher = {American Society for Cell Biology (ASCB)},
month = {jan},
url = {https://doi.org/10.1091%2Fmbc.E02-06-0327},
number = {1},
pages = {1--13},
doi = {10.1091/mbc.E02-06-0327}
}
MLA
Cite this
MLA Copy
Friedman, Katherine L., et al. “N-terminal Domain of Yeast Telomerase Reverse Transcriptase: Recruitment of Est3p to the Telomerase Complex.” Molecular Biology of the Cell, vol. 14, no. 1, Jan. 2003, pp. 1-13. https://doi.org/10.1091%2Fmbc.E02-06-0327.
Found error?