The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states
NATURE STRUCTURAL & MOLECULAR BIOLOGY（2009）
摘要
Telomeres alternate between telomerase-extendable and telomerase-unextendable states. Now this switch is reconstituted in vitro , using DNA templates and purified telomeric proteins from yeast. The molecular chaperone Hsp82 is shown to have a role in this switch by modulating the DNA binding activity of Cdc13.
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关键词
molecular chaperone,rna,mechanism,apoptosis,protein folding,rna processing,nucleic acids,cell cycle,chromatin,proteins,biophysics,genetics,n terminal,rnai,macromolecules,molecular biology,chromatin structure,signal transduction,gene expression,molecular,dna recombination,telomerase,transcription,chromatin remodeling,enzyme activation,cell biology,dna repair,biochemistry,dna replication,translation,telomere
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