TRF1, a mammalian telomeric protein

Telomerase adds TTAGGG repeats onto mammalian chromosome ends, replenishing the terminal sequence loss incurred during DNA replication. This maintenance of telomeric DNA preserves binding sites for telomeric proteins, which form a protective nucleoprotein complex at chromosome ends. The recent isola...

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Bibliographic Details
Published in:Trends in Genetics 1997, Vol.13 (1), p.21-26
Main Authors: Smith, Susan, de Lange, Titia
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Biological and medical sciences
Chromatin. Chromosome
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Genes, Tumor Suppressor
Humans
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Oncogene Proteins v-myb
Protein Conformation
Repetitive Sequences, Nucleic Acid
Retroviridae Proteins, Oncogenic - metabolism
Sequence Homology, Amino Acid
Telomere - chemistry
Telomere - metabolism
Telomeric Repeat Binding Protein 1
Transcription Factors - genetics
Transcription Factors - metabolism
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Summary:Telomerase adds TTAGGG repeats onto mammalian chromosome ends, replenishing the terminal sequence loss incurred during DNA replication. This maintenance of telomeric DNA preserves binding sites for telomeric proteins, which form a protective nucleoprotein complex at chromosome ends. The recent isolation of TRF1, the mammalian telomeric-repeat binding factor, should now allow the structure and function of the telomeric complex to be examined in detail.
ISSN:0168-9525
DOI:10.1016/S0168-9525(96)10052-4