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Related Experiment Videos

Characterization of amplified intracisternal A-particle elements encoding integrase.

K K Lueders1, Z Grossman, J W Fewell

  • 1Laboratory of Biochemistry, National Cancer Institute, Bethesda, MD 20892.

Nucleic Acids Research
|November 25, 1989
PubMed
Summary

Type IIB intracisternal A-particle (IAP) elements amplify in mouse myeloma DNA. Researchers identified the IAP integrase enzyme, crucial for integrating proviral DNA, and detected it in myeloma cells.

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Area of Science:

  • Molecular Biology
  • Genomics
  • Virology

Background:

  • Type IIB intracisternal A-particle (IAP) elements exhibit significant amplification and transposition in the genomic DNA of specific mouse myelomas.
  • The molecular mechanisms driving this amplification and transposition remain incompletely understood.

Purpose of the Study:

  • To investigate whether intrinsic properties of Type IIB IAP elements contribute to their amplification in mouse myelomas.
  • To identify and characterize potential proteins involved in IAP transposition.

Main Methods:

  • Construction of a cDNA library from MOPC 315 mouse myeloma cells.
  • Sequencing of Type IIB IAP cDNAs and genomic elements.
  • Expression of IAP integrase in bacteria and generation of antiserum.

Related Experiment Videos

  • Western blot analysis of myeloma cell fractions.

    • Main Results:

    • Type IIB IAP cDNAs and genomic elements were found to be highly similar (>99%).
    • Two open reading frames (ORFs) were identified, with ORF2 encoding the IAP integrase.
    • Antiserum confirmed the identity of the ORF2 product and detected a 47 kDa protein in myeloma cell fractions.

    Conclusions:

    • The IAP integrase, encoded by ORF2, is a key enzyme for proviral DNA integration.
    • The presence and detection of the IAP integrase protein in myeloma cells suggest its role in IAP amplification and transposition.