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Mutational analysis of the carboxyl terminus of the Moloney murine leukemia virus integration protein

M J Roth1

  • 1Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854-5635.

Journal of Virology
|April 1, 1991
PubMed

Insights

The Moloney murine leukemia virus integration protein (IN) C terminus is not essential for retrovirus DNA integration. Specific insertions within the IN protein also yield viable viruses, indicating functional flexibility.

Area of Science:

  • Molecular Biology
  • Virology
  • Genetics

Background:

  • Retrovirus DNA integration into host genomes is a critical step mediated by the integration protein (IN).
  • Understanding the functional domains of retroviral IN proteins is crucial for deciphering viral replication mechanisms.

Purpose of the Study:

  • To investigate the role of the C-terminal region of the Moloney murine leukemia virus (MMLV) integration protein (IN).
  • To determine the impact of specific amino acid insertions on MMLV IN function and viral viability.

Main Methods:

  • Functional analysis of the MMLV IN protein C terminus.
  • Genetic manipulation involving linker insertion within the MMLV IN gene at position 6025.

Main Results:

  • The terminal 28 amino acids of the MMLV IN protein were identified as nonessential for viral function.
  • A viable virus was produced despite a 36-amino-acid insertion at position 6025 within the IN protein, a unique feature among retroviruses.

Conclusions:

  • The C terminus of MMLV IN is dispensable for DNA integration and virus viability.
  • The MMLV IN protein tolerates significant structural modifications, suggesting potential plasticity in its functional domains.

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