Abstract
The telomere environment requires an efficient means to assemble and disassemble a multitude of structures to operate correctly and to help achieve cellular homeostasis. Telomeres are challenged by a common binding specificity displayed by many of the protein components for telomeric DNA, which could result in competitive DNA interactions, and by a cell cycle-restricted timing of events, which enforces a narrow working period in which to perform numerous tasks. In this review, we discuss how the HSP90 molecular chaperone network avoids these obstacles and facilitates an effective operation of the telomere system.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 384-391 |
| Number of pages | 8 |
| Journal | Trends in Biochemical Sciences |
| Volume | 35 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jul 1 2010 |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
Cite this
HSP90 manages the ends. / DeZwaan, Diane C.; Freeman, Brian C.
In: Trends in Biochemical Sciences, Vol. 35, No. 7, 01.07.2010, p. 384-391.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - HSP90 manages the ends
AU - DeZwaan, Diane C.
AU - Freeman, Brian C
PY - 2010/7/1
Y1 - 2010/7/1
N2 - The telomere environment requires an efficient means to assemble and disassemble a multitude of structures to operate correctly and to help achieve cellular homeostasis. Telomeres are challenged by a common binding specificity displayed by many of the protein components for telomeric DNA, which could result in competitive DNA interactions, and by a cell cycle-restricted timing of events, which enforces a narrow working period in which to perform numerous tasks. In this review, we discuss how the HSP90 molecular chaperone network avoids these obstacles and facilitates an effective operation of the telomere system.
AB - The telomere environment requires an efficient means to assemble and disassemble a multitude of structures to operate correctly and to help achieve cellular homeostasis. Telomeres are challenged by a common binding specificity displayed by many of the protein components for telomeric DNA, which could result in competitive DNA interactions, and by a cell cycle-restricted timing of events, which enforces a narrow working period in which to perform numerous tasks. In this review, we discuss how the HSP90 molecular chaperone network avoids these obstacles and facilitates an effective operation of the telomere system.
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UR - http://www.scopus.com/inward/citedby.url?scp=77954315404&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2010.02.005
DO - 10.1016/j.tibs.2010.02.005
M3 - Review article
C2 - 20236825
AN - SCOPUS:77954315404
VL - 35
SP - 384
EP - 391
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
SN - 0376-5067
IS - 7
ER -