Implication of a Central Cysteine Residue and the HHCC Domain of Moloney Murine Leukemia Virus Integrase Protein in Functional Multimerization

  1. Monica J. Roth1,*
  1. Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854,1 and
  2. Instituto de Bioquimica, Facultad de Ciencias, Universidad Austral de Chile, Casilla 567, Valdivia, Chile2

ABSTRACT

Moloney murine leukemia virus (M-MuLV) IN-IN protein interactions important for catalysis of strand transfer and unimolecular and bimolecular disintegration reactions were investigated by using a panel of chemically modified M-MuLV IN proteins. Functional complementation of an HHCC-deleted protein (NΔ105) by an independent HHCC domain (CΔ232) was severely compromised by NEM modification of either subunit. Productive NΔ105 IN-DNA interactions with a disintegration substrate lacking a long terminal repeat 5′-single-stranded tail also required complementation by a functional HHCC domain. Virus encoding the C209A M-MuLV IN mutation exhibited delayed virion production and replication kinetics.

FOOTNOTES

    • Received 11 July 1997.
    • Accepted 21 October 1997.

  • ↵* Corresponding author. Mailing address: Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, 675 Hoes Ln., Piscataway, NJ 08854. Phone: (732) 235-5048. Fax: (732) 235-4783. E-mail:Roth{at}mbcl.rutgers.edu.

  • ↵† Present address: Aaron Diamond AIDS Research Center, New York, NY 10019.

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  1. J. Virol. vol. 72 no. 2 1691-1698
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