Journal article
Mapping the FEN1 interaction domain with hTERT
Biochemical and biophysical research communications, Vol.407(1), pp.34-38
04/01/2011
Handle:
https://hdl.handle.net/2376/110399
PMCID: PMC3070821
PMID: 21345332
Abstract
The activity of telomerase in cancer cells is tightly regulated by numerous proteins including DNA replication factors. However, it is unclear how replication proteins regulate telomerase action in higher eukaryotic cells. Previously we have demonstrated that the multifunctional DNA replication and repair protein flap endonuclease 1 (FEN1) is in complex with telomerase and may regulate telomerase activity in mammalian cells. In this study, we further analyzed the nature of this association. Our results show that FEN1 and telomerase association occurs throughout the S phase, with the maximum association in the mid S phase. We further mapped the physical domains in FEN1 required for this association and found that the C terminus and the nuclease domain of FEN1 are involved in this interaction, whereas the PCNA binding ability of FEN1 is dispensable for the interaction. These results provide insights into the nature of possible protein-protein associations that telomerase participates in for maintaining functional telomeres.
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Details
- Title
- Mapping the FEN1 interaction domain with hTERT
- Creators
- Shilpa Sampathi - WWAMI Medical Education Program, Washington State University, Spokane, WA 99210Weihang Chai - WWAMI Medical Education Program, Washington State University, Spokane, WA 99210
- Publication Details
- Biochemical and biophysical research communications, Vol.407(1), pp.34-38
- Academic Unit
- UNKNOWN
- Identifiers
- 99900546919301842
- Language
- English
- Resource Type
- Journal article