| Literature DB >> 9445080 |
G A Donzella1, O Leon, M J Roth.
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 (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.Entities:
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Year: 1998 PMID: 9445080 PMCID: PMC124658
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103