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

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.

journal_name

J Virol

journal_title

Journal of virology

authors

Donzella GA,Leon O,Roth MJ

doi

10.1128/JVI.72.2.1691-1698.1998

subject

Has Abstract

pub_date

1998-02-01 00:00:00

pages

1691-8

issue

2

eissn

0022-538X

issn

1098-5514

journal_volume

72

pub_type

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