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Telomere architecture.
Rhodes, Daniela; Fairall, Louise; Simonsson, Tomas; Court, Robert; Chapman, Lynda.
Affiliation
  • Rhodes D; MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. rhodes@mrc-lmb.cam.ac.uk
EMBO Rep ; 3(12): 1139-45, 2002 Dec.
Article in En | MEDLINE | ID: mdl-12475927
Telomeres are protein-DNA complexes that cap chromosome ends and protect them from being recognized and processed as DNA breaks. Loss of capping function results in genetic instability and loss of cellular viability. The emerging view is that maintenance of an appropriate telomere structure is essential for function. Structural information on telomeric proteins that bind to double and single-stranded telomeric DNA shows that, despite a lack of extensive amino-acid sequence conservation, telomeric DNA recognition occurs via conserved DNA-binding domains. Furthermore, telomeric proteins have multidomain structures and hence are conformationally flexible. A possibility is that telomeric proteins take up different conformations when bound to different partners, providing a simple mechanism for modulating telomere architecture.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: DNA / Telomere / Homeodomain Proteins / Oncogene Proteins v-myb Limits: Animals Language: En Journal: EMBO Rep Journal subject: BIOLOGIA MOLECULAR Year: 2002 Document type: Article Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: DNA / Telomere / Homeodomain Proteins / Oncogene Proteins v-myb Limits: Animals Language: En Journal: EMBO Rep Journal subject: BIOLOGIA MOLECULAR Year: 2002 Document type: Article Country of publication: United kingdom