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Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein
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Structural basis for protein-RNA recognition in telomerase.

Jing Huang1, Andrew F Brown2, Jian Wu3

  • 11] National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China. [2] Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor, Michigan, USA. [3] Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, USA.

Nature Structural & Molecular Biology
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Researchers elucidated the structure of telomerase components, revealing how telomerase reverse transcriptase (TERT) binds to telomerase RNA (TR). This structural insight into TERT-TR interaction is crucial for understanding telomerase assembly and function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Telomerase is a ribonucleoprotein enzyme essential for maintaining telomere length.
  • The catalytic subunit is telomerase reverse transcriptase (TERT), and the RNA component is TR.
  • The precise assembly mechanism of TERT and TR into a functional telomerase remains largely unknown.

Purpose of the Study:

  • To determine the structural basis of telomerase reverse transcriptase (TERT) and telomerase RNA (TR) interaction.
  • To investigate the role of conserved regions 4 and 5 (CR4/5) of TR in binding to the TR-binding domain (TRBD) of TERT.

Main Methods:

  • X-ray crystallography was used to determine the structure of the TR CR4/5 and TERT TRBD complex.
  • Mutational analyses were performed to assess the importance of sequence and conformation in the interaction.

Main Results:

  • The crystal structure revealed an L-shaped conformation of TR CR4/5 that clamps onto the TERT TRBD.
  • Both the sequence and the specific L-shaped conformation of CR4/5 are critical for TERT binding.
  • The interaction mode suggests conservation across most eukaryotes.

Conclusions:

  • The CR4/5-TRBD interaction provides a structural foundation for telomerase assembly.
  • Vertebrate TR CR4/5 may play a regulatory role analogous to Tetrahymena TR stem-loop IV.
  • This study offers insights into the fundamental mechanisms of telomerase biogenesis and regulation.