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Related Experiment Videos

Rec (formerly Corf) function requires interaction with a complex, folded RNA structure within its responsive element

C Magin-Lachmann1, S Hahn, H Strobel

  • 1Paul-Ehrlich-Institut, D-63225 Langen, Germany.

Journal of Virology
|October 3, 2001
PubMed
Summary

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Human endogenous retrovirus HTDV/HERV-K’s Rec protein binds RNA structures, not specific sites, unlike HIV Rev and HTLV Rex. This finding clarifies Rec’s nuclear export mechanism and HERV-K regulation.

Area of Science:

  • Molecular Biology
  • Virology
  • Genomics

Background:

  • Human endogenous retroviruses (HERVs) are remnants of ancient retroviral infections in the human genome.
  • HTDV/HERV-K encodes the regulatory protein Rec, analogous to HIV Rev and HTLV Rex, involved in nuclear export.
  • Rec interacts with a specific RNA element, the Rec-responsive element (RcRE), in HTDV/HERV-K transcripts.

Purpose of the Study:

  • To investigate the RNA binding characteristics of the HTDV/HERV-K Rec protein.
  • To determine if Rec binds to a discrete site within the RcRE, similar to Rev and Rex.
  • To identify structural features of the RcRE essential for Rec function.

Main Methods:

  • Analysis of HTDV/HERV-K genomic copies to identify active RcREs.
  • Site-directed mutagenesis to characterize mutations affecting Rec function.

Related Experiment Videos

  • RNA structure probing and functional assays to define Rec-RcRE interactions.

    • Main Results:

    • Not all HTDV/HERV-K copies possess an active RcRE.
    • Rec function depends on binding to a complex, folded RNA structure, not a discrete site.
    • Four essential stem-loop structures within the RcRE were identified.
    • Both Rev and Rex can utilize the RcRE for nuclear export, but with distinct binding interactions.

    Conclusions:

    • HTDV/HERV-K Rec's RNA binding mechanism differs from HIV Rev and HTLV Rex.
    • Rec's interaction with a structured RcRE is crucial for its regulatory function.
    • The RcRE's structural plasticity allows interaction with different viral export proteins.