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Related Experiment Videos

Trimeric structure for an essential protein in L1 retrotransposition.

Sandra L Martin1, Dan Branciforte, David Keller

  • 1Department of Cell and Developmental Biology and Program in Molecular Biology, University of Colorado School of Medicine, 4200 East Ninth Avenue, Denver, CO 80262, USA. sandy.martin@uchsc.edu

Proceedings of the National Academy of Sciences of the United States of America
|November 15, 2003
PubMed
Summary

Mouse LINE-1 ORF1p protein structure was investigated. Full-length protein forms an asymmetric trimer, while the C-terminal domain is a monomer, explaining its nucleic acid chaperone function.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Mammalian retrotransposon LINE-1 (L1) encodes two essential proteins for retrotransposition.
  • The function of ORF1p, encoded by the 5'-most open reading frame, is not fully understood.
  • Mouse L1 ORF1p binds single-stranded nucleic acids and acts as a nucleic acid chaperone.

Purpose of the Study:

  • To elucidate the structure of full-length mouse L1 ORF1p and its C-terminal domain (C-1/3).
  • To correlate structural features with the known nucleic acid binding and chaperone activities of L1 ORF1p.

Main Methods:

  • Purification of full-length and C-1/3 domains of mouse L1 ORF1p.
  • Analysis using gel filtration chromatography and analytical ultracentrifugation.
  • Structural examination via atomic force microscopy.

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Main Results:

  • Both full-length and C-1/3 proteins were structurally homogeneous and asymmetric in solution.
  • Full-length ORF1p formed a stable trimer, whereas the C-1/3 domain remained a monomer.
  • Atomic force microscopy revealed an asymmetric dumbbell shape for full-length ORF1p.

Conclusions:

  • The determined structural features, including the trimeric state of full-length ORF1p and monomeric C-1/3 domain, are consistent with its nucleic acid binding and chaperone activities.
  • These findings provide structural insights into the function of L1 ORF1p during LINE-1 retrotransposition.