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J Mol Biol. 2011 Jul 1;410(1):10-7. doi: 10.1016/j.jmb.2011.04.049. Epub 2011 May 9.

Multiple POT1-TPP1 proteins coat and compact long telomeric single-stranded DNA.

Author information

  • 1Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA. derek.taylor@case.edu

Abstract

Telomeres are nucleoprotein complexes that cap and protect the ends of linear chromosomes. In humans, telomeres end in 50-300 nt of G-rich single-stranded DNA (ssDNA) overhangs. Protection of telomeres 1 (POT1) binds with nanomolar affinity to the ssDNA overhangs and forms a dimer with another telomere-end binding protein called TPP1. Whereas most previous studies utilized telomeric oligonucleotides comprising single POT1-TPP1 binding sites, here, we examined 72- to 144-nt tracts of telomeric DNA containing 6-12 POT1-TPP1 binding sites. Using electrophoretic mobility gel shift assays, size-exclusion chromatography, and electron microscopy, we analyzed telomeric nucleoprotein complexes containing POT1 alone, POT1-TPP1, and a truncated version of POT1 (POT1-N) that maintains its DNA-binding domain. The results revealed that POT1-N and POT1-TPP1 can completely coat long telomeric ssDNA substrates. Furthermore, we show that ssDNA coated with human POT1-TPP1 heterodimers forms compact, potentially ordered structures.

Copyright © 2011 Elsevier Ltd. All rights reserved.

PMID:
21596049
[PubMed - indexed for MEDLINE]
PMCID:
PMC3157753
Free PMC Article
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