Implication of a central cysteine residue and the HHCC domain of Moloney murine leukemia virus integrase protein in functional multimerization.
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 (Ndelta105) by an independent HHCC domain (Cdelta232) was severely compromised by NEM modification of either subunit. Productive Ndelta105 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.
Donzella
G A
GA
Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway 08854, USA.
Leon
O
O
Roth
M J
MJ
D000818:Animals; D019281:Dimerization; D019426:Integrases / Q000235:genetics* / Q000378:metabolism; D009052:Leukemia Virus, Murine / Q000502:physiology*; D051379:Mice; D017384:Sequence Deletion; D014779:Virus Replication / Q000235:genetics
D019426:Integrases