Different role of functional domains of hTR in DNA binding to telomere and telomerase reconstruction

M. Yeo, S. Y. Rha, H. C. Jeung, X. H. Shen, S. H. Yang, S. W. An, J. K. Roh, H. C. Chung

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

Even if template sequence of hTR played an essential role in telomere binding, a 326 nucleotide fragment of hTR containing template, pseudoknot, and CR4-5 domains is critical for both binding with telomeric DNA and reconstitution of telomerase activity. A functional study with antisense oligonucleotides suggested that targeted disruption of the template region efficiently abrogated both telomeric DNA binding and telomerase activity, whereas disruption of the CR4-5 region induced only loss of telomerase activity. hTR interacts with telomeric DNA via structural region composed of the template, pseudoknot, and CR4-5 domains, however, each structural domain plays a distinct role in telomere binding and telomerase activity reconstitution.

Original languageEnglish
Pages (from-to)127-132
Number of pages6
JournalFEBS Letters
Volume579
Issue number1
DOIs
Publication statusPublished - 2005 Jan 3

Bibliographical note

Funding Information:
This work was supported by the Korea Sciences and Engineering Fund through the Cancer Metastasis Research Center at Yonsei University. We thank S.C. Kim for the gift of hTERT cDNA and S.T. Kim for his helpful discussions and his reading of the manuscript.

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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