PMID: 9445080Jan 28, 1998Paper

Implication of a central cysteine residue and the HHCC domain of Moloney murine leukemia virus integrase protein in functional multimerization

Journal of Virology
G A DonzellaM 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.

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Citations

Dec 23, 2009·Archives of Biochemistry and Biophysics·Mónica L AcevedoOscar León

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