Pot1, the putative telomere end-binding protein in fission yeast and humans

Science. 2001 May 11;292(5519):1171-5. doi: 10.1126/science.1060036.

Abstract

Telomere proteins from ciliated protozoa bind to the single-stranded G-rich DNA extensions at the ends of macronuclear chromosomes. We have now identified homologous proteins in fission yeast and in humans. These Pot1 (protection of telomeres) proteins each bind the G-rich strand of their own telomeric repeat sequence, consistent with a direct role in protecting chromosome ends. Deletion of the fission yeast pot1+ gene has an immediate effect on chromosome stability, causing rapid loss of telomeric DNA and chromosome circularization. It now appears that the protein that caps the ends of chromosomes is widely dispersed throughout the eukaryotic kingdom.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Chromosome Segregation / genetics
  • Chromosomes, Fungal / genetics
  • Chromosomes, Fungal / metabolism
  • Cloning, Molecular
  • DNA / genetics
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Electrophoresis, Gel, Pulsed-Field
  • Female
  • Gene Deletion
  • Gene Expression Profiling
  • Heterozygote
  • Humans
  • Molecular Sequence Data
  • Ovary / metabolism
  • Phenotype
  • RNA, Messenger / analysis
  • RNA, Messenger / genetics
  • Schizosaccharomyces / genetics*
  • Schizosaccharomyces pombe Proteins
  • Sequence Alignment
  • Substrate Specificity
  • Telomere / genetics
  • Telomere / metabolism*
  • Telomere-Binding Proteins*

Substances

  • DNA-Binding Proteins
  • POT1 protein, human
  • RNA, Messenger
  • Schizosaccharomyces pombe Proteins
  • Telomere-Binding Proteins
  • pot1 protein, S pombe
  • DNA