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Related Experiment Videos

Nucleolin interacts with telomerase.

Shilagardi Khurts1, Kenkichi Masutomi, Luvsanjav Delgermaa

  • 1Department of Molecular Biology, Cancer Research Institute, Kanazawa University, Kanazawa 920-0934, Japan.

The Journal of Biological Chemistry
|September 17, 2004
PubMed
Summary
This summary is machine-generated.

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Nucleolin protein interacts with telomerase and its core subunits, human telomerase reverse transcriptase (hTERT) and telomerase RNA (hTERC). This interaction is crucial for regulating telomerase

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Telomerase is a ribonucleoprotein enzyme essential for maintaining telomere length in dividing cells.
  • Telomerase activity is tightly regulated and involves dynamic subcellular localization.
  • Telomerase has been observed to colocalize with nucleoli in human cells.

Purpose of the Study:

  • To investigate the interaction between nucleolin and telomerase components.
  • To determine the role of nucleolin in the subcellular localization of telomerase.

Main Methods:

  • Co-immunoprecipitation assays to detect protein-protein interactions.
  • Immunofluorescence microscopy to visualize subcellular localization.
  • Analysis of protein domains involved in the interaction.

Related Experiment Videos

Main Results:

  • Nucleolin directly interacts with the human telomerase reverse transcriptase subunit (hTERT) and the telomerase RNA component (hTERC).
  • Nucleolin binds hTERT via its RNA binding domain 4 and carboxyl-terminal RGG domain.
  • This interaction is essential for the nucleolar localization of hTERT.

Conclusions:

  • Nucleolin acts as a key regulator of telomerase subcellular localization.
  • The interaction between nucleolin and hTERT influences the dynamic intracellular trafficking of the telomerase complex.
  • These findings provide new insights into the regulation of telomerase function.