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Updated: Feb 16, 2026

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Dissection of affinity captured LINE-1 macromolecular complexes.

Martin S Taylor1, Ilya Altukhov2, Kelly R Molloy3

  • 1Department of Pathology, Massachusetts General Hospital, Boston, United States.

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|January 9, 2018
PubMed
Summary

Mobile genetic elements called Long Interspersed Nuclear Element-1 (LINE-1, L1) utilize proteins to form complexes. Researchers identified distinct cytoplasmic and nuclear L1-protein complexes, revealing new insights into their activity.

Keywords:
LINE-1affinity proteomicsbiochemistrychemical biologycomputational biologyhumaninteractomeretrotransposonribonucleoproteinsystems biology

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Area of Science:

  • Genetics
  • Molecular Biology
  • Genomics

Background:

  • Long Interspersed Nuclear Element-1 (LINE-1, L1) are mobile genetic elements active in human genomes.
  • L1 elements encode ORF1 and ORF2 proteins that bind L1 RNAs, forming ribonucleoproteins (RNPs).
  • These RNPs interact with various host proteins, influencing L1 activity.

Purpose of the Study:

  • To characterize the proteins and nucleic acids associated with enzymatically active L1 macromolecular complexes.
  • To identify distinct L1 RNP intermediates in the cytoplasm and nucleus.
  • To understand the composition of L1 complexes involved in target-primed reverse transcription.

Main Methods:

  • Differential affinity purifications.
  • Quantitative mass spectrometry.
  • Next-generation RNA sequencing.

Main Results:

  • Distinct, enzymatically active L1 macromolecular complexes were characterized.
  • A cytoplasmic intermediate containing ORF1p, ORF2p, and L1 RNA was identified.
  • A nuclear L1 population containing ORF2p but lacking ORF1p was observed, potentially involved in reverse transcription.

Conclusions:

  • The study identified distinct cytoplasmic and nuclear L1 ribonucleoprotein complexes.
  • These findings provide a deeper understanding of L1 RNP composition and function.
  • The identified complexes offer insights into the mechanisms of L1 retrotransposition and host interactions.