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J Virol, February 1998, p. 1691-1698, Vol. 72, No. 2
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

George A. Donzella,1,dagger Oscar Leon,2 and Monica J. Roth1,*

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

Received 11 July 1997/Accepted 21 October 1997

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 (NDelta 105) by an independent HHCC domain (CDelta 232) was severely compromised by NEM modification of either subunit. Productive NDelta 105 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.

* 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.

dagger Present address: Aaron Diamond AIDS Research Center, New York, NY 10019.




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