ArticleNature structural & molecular biology2009
The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 47 citations in OpenAlex.
- Establishing Order Through Disorder by the Hsp90 Molecular Chaperone.Journal of molecular biology · 2024Review
- Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024Review
- Organismal Roles of Hsp90.Biomolecules · 2023Review
- Assessment of Post-Radiation Time Effect on Gene Expression Profiles ofJournal of lasers in medical sciences · 2021Article
- Possible Involvement of Hsp90 in the Regulation of Telomere Length and Telomerase Activity During theFrontiers in cell and developmental biology · 2021Article
- The Nuclear and DNA-Associated Molecular Chaperone Network.Cold Spring Harbor perspectives in biology · 2019Review
- The HSP90 chaperone machinery.Nature reviews. Molecular cell biology · 2017Review
- Functional characterisation of long intergenic non-coding RNAs through genetic interaction profiling in Saccharomyces cerevisiae.BMC biology · 2016Article
- Modulation of yeast telomerase activity by Cdc13 and Est1 in vitro.Scientific reports · 2016Article
- Dynamic Interactions of Arabidopsis TEN1: Stabilizing Telomeres in Response to Heat Stress.The Plant cell · 2016Article
- Structure and function of the telomeric CST complex.Computational and structural biotechnology journal · 2016Review
- Proteomics of yeast telomerase identified Cdc48-Npl4-Ufd1 and Ufd4 as regulators of Est1 and telomere length.Nature communications · 2015Article
- Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.Eukaryotic cell · 2015Article
- Coordination of transposon expression with DNA replication in the targeting of telomeric retrotransposons in Drosophila.The EMBO journal · 2014Article
- Cdk1 regulates the temporal recruitment of telomerase and Cdc13-Stn1-Ten1 complex for telomere replication.Molecular and cellular biology · 2014Article
- Human TEN1 maintains telomere integrity and functions in genome-wide replication restart.The Journal of biological chemistry · 2013Article
- Cdc13 OB2 dimerization required for productive Stn1 binding and efficient telomere maintenance.Structure (London, England : 1993) · 2013Article
- Structure of the human telomeric Stn1-Ten1 capping complex.PloS one · 2013Article
- The therapeutic target Hsp90 and cancer hallmarks.Current pharmaceutical design · 2013Review
- Everything you ever wanted to know about Saccharomyces cerevisiae telomeres: beginning to end.Genetics · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Distinct protein assemblies are nucleated at telomeric DNA to both guard the ends from damage and lengthen the DNA after replication. In yeast, Cdc13 recruits either Stn1-Ten1 to form a protective cap or the telomerase holoenzyme to extend the DNA. We have established an in vitro yeast telomere system in which Stn1-Ten1-unextendable or telomerase-extendable states can be observed. Both assemblies are Cdc13 dependent, as the Cdc13 C-terminal region supports Stn1-Ten1 interactions and the N-terminal region contains a telomerase-activation function. Notably, the yeast Hsp90 chaperone Hsp82 mediates the switch between the telomere capping and extending structures by modulating the DNA binding activity of Cdc13. Taken together, our data show that the Hsp82 chaperone facilitates telomere DNA maintenance by promoting transitions between two operative complexes and by reducing the potential for binding events that would otherwise block the assembly of downstream structures.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.