The POT1-TPP1 telomere complex is a telomerase processivity factor
Article Abstract:
The crystal structure of a domain of human TPP1 has disclosed an oilgonucleotide/oligosaccharide-binding fold that is structurally similar to the [beta]-subunit of the telomere end-binding protein of a ciliated protozoan, indicating that TPP1 is the missing [beta]-subunit of human protection of telomeres (POT1) protein. The results have proposed that POT1-TPP1has switched from inhibiting telomerase access to the telomere, as a component of shelterin, in order to serve as a processivity factor for telomerase during telomerase extension.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
User Contributions:
Comment about this article or add new information about this topic:
Dangerous liaisons
Article Abstract:
Two theories are proposed to explain as to how the immune system is recruited to active duty. Uric acid released by damaged cells is a danger signal that is able to notify immune cells of microbial attack.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Structure of the Escherichia coli ribosomal termination complex with release factor 2. Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo
- Abstracts: The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production
- Abstracts: Quake aid hampered by ban on web shots. Japan consoled with contracts as France snares fusion project. Quake triggeres research expedition
- Abstracts: From hive minds to humans. Ubiquitination by the anaphase-promoting complex drives spindle checkpoint inactivation
- Abstracts: Sperm chromatin proteomics identifies evolutionary conserved fertility factors. Social interactions among epithelial cells during tracheal branching morphogenesis