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MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, U.K.
The herpes simplex virus type 1 origin-binding protein is encoded by gene UL9. We previously described a plasmid, pB1, which encodes a fusion protein containing only the C-terminal 317 amino acids of the UL9 polypeptide and showed that this product retains sequence-specific DNA-binding ability. Two series of pB1 mutants have now been constructed and the polypeptides were tested for origin-binding activity. Using C-terminal truncations, we show that the C-terminal 34 amino acids of UL9 are dispensable for binding and that essential residues lie between positions 801 and 818. Analysis of a series of mutants containing insertions of four amino acids at various positions identified regions of the DNA-binding domain in which alterations either abolished or had relatively little effect upon binding activity. Two mutants which were intermediate in their binding activities also exhibited temperature- or sequence-specific effects.
Received 14 December 1992;
accepted 15 February 1993.
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B. Marintcheva and S. K. Weller Residues within the Conserved Helicase Motifs of UL9, the Origin-binding Protein of Herpes Simplex Virus-1, Are Essential for Helicase Activity but Not for Dimerization or Origin Binding Activity J. Biol. Chem., February 23, 2001; 276(9): 6605 - 6615. [Abstract] [Full Text] [PDF]
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