Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection

The POT1 (protection of telomeres 1) protein binds the single-stranded overhang at the ends of chromosomes in diverse eukaryotes. It is essential for chromosome end-protection in the fission yeast Schizosaccharomyces pombe, and it is involved in regulation of telomere length in human cells. Here, we...

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Published inNature structural & molecular biology Vol. 11; no. 12; pp. 1223 - 1229
Main Authors Cech, Thomas R, Lei, Ming, Podell, Elaine R
Format Journal Article
LanguageEnglish
Published United States Nature Publishing Group 01.12.2004
Subjects
Base Sequence
Cell cycle
Chromosomes
Crystal structure
Crystallography, X-Ray
Deoxyribonucleic acid
DNA
DNA binding proteins
DNA, Single-Stranded - chemistry
DNA, Single-Stranded - genetics
DNA, Single-Stranded - metabolism
Genetic aspects
Genomes
Humans
Models, Biological
Models, Molecular
Nucleic Acid Conformation
Physiological aspects
Protein Binding
Protein Structure, Tertiary
Protein-protein interactions
Proteins
Schizosaccharomyces pombe
Schizosaccharomyces pombe Proteins
Structure
Telomerase
Telomerase - metabolism
Telomere - chemistry
Telomere - genetics
Telomere - metabolism
Telomere-Binding Proteins - chemistry
Telomere-Binding Proteins - metabolism
Telomeres
Yeast
Yeasts
United States
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Summary:The POT1 (protection of telomeres 1) protein binds the single-stranded overhang at the ends of chromosomes in diverse eukaryotes. It is essential for chromosome end-protection in the fission yeast Schizosaccharomyces pombe, and it is involved in regulation of telomere length in human cells. Here, we report the crystal structure at a resolution of 1.73 A of the N-terminal half of human POT1 (hPOT1) protein bound to a telomeric single-stranded DNA (ssDNA) decamer, TTAGGGTTAG, the minimum tight-binding sequence indicated by in vitro binding assays. The structure reveals that hPOT1 contains two oligonucleotide/ oligosaccharide-binding (OB) folds; the N-terminal OB fold binds the first six nucleotides, resembling the structure of the S. pombe Pot1pN-ssDNA complex, whereas the second OB fold binds and protects the 3' end of the ssDNA. These results provide an atomic-resolution model for chromosome end-capping.
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ISSN:1545-9993
1545-9985
DOI:10.1038/nsmb867