Interaction of human Ku70 with TRF2
Open Access
- 6 September 2000
- journal article
- Published by Wiley in FEBS Letters
- Vol. 481 (1), 81-85
- https://doi.org/10.1016/s0014-5793(00)01958-x
Abstract
Ku, a heterodimer of 70‐ and 80‐kDa subunits, plays a general role in the metabolism of DNA ends in eukaryotic cells, including double‐strand DNA break repair, V(D)J recombination, and maintenance of telomeres. We have utilized the yeast two‐hybrid system to identify Ku70‐interacting proteins other than Ku80. Two reactive clones were found to encode the dimerization domain of TRF2, a mammalian telomeric protein that binds to duplex TTAGGG repeats at chromosome ends. This interaction was confirmed using bacterial fusion proteins and co‐immunoprecipitations from eukaryotic cells overexpressing TRF2. The transfected TFR2 colocalized with Ku70.Keywords
This publication has 32 references indexed in Scilit:
- Characteristic Immunolocalization of Ku Protein as Nuclear MatrixHybridoma, 1998
- Assignment1 of a human putative RNA helicase gene, DDX3, to human X chromosome bands p11.3→p11.23Cytogenetic and Genome Research, 1998
- Human telomeres contain two distinct Myb–related proteins, TRF1 and TRF2Nature Genetics, 1997
- Telomeric localization of TRF2, a novel human telobox proteinNature Genetics, 1997
- Absence of p350 Subunit of DNA-Activated Protein Kinase from a Radiosensitive Human Cell LineScience, 1995
- DNA-dependent protein kinase activity is absent in xrs-6 cells: implications for site-specific recombination and DNA double-strand break repair.Proceedings of the National Academy of Sciences of the United States of America, 1995
- Involvement of the Ku autoantigen in the cellular response to DNA double-strand breaks.Proceedings of the National Academy of Sciences of the United States of America, 1994
- Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2Cell, 1993
- The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding ProteinsScience, 1988
- Characterization of a high molecular weight acidic nuclear protein recognized by autoantibodies in sera from patients with polymyositis-scleroderma overlap.JCI Insight, 1981