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M205984200v1
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Papers In Press, published online ahead of print August 30, 2002
J. Biol. Chem, 10.1074/jbc.M205984200
Submitted on June 17, 2002
Revised on August 23, 2002
Accepted on August 30, 2002

Structure-function analysis of Escherichia coli DNA helicase I reveals non-overlapping transesterase and helicase domains

Devon R. Byrd, Juliana K. Sampson, Heather Ragonese, and Steven W. Matson

Biology Dept., University of North Carolina, Chapel Hill, NC 27599-3280

Corresponding Author: smatson{at}bio.unc.edu

TraI (DNA helicase I) is an Escherichia coli F plasmid-encoded protein required for bacterial conjugative DNA transfer. The protein is a sequence-specific DNA transesterase that provides the site- and strand-specific nick required to initiate DNA strand transfer and a 5' to 3' DNA helicase that unwinds the F plasmid to provide the single-stranded DNA that is transferred from donor to recipient. Sequence comparisons with other transesterases and helicases suggest that these activities reside in the amino- and carboxyl-terminal regions of TraI, respectively. Computer-assisted secondary structure probability analysis identified a potential interdomain region spanning residues 304-309. Proteins encoded by segments of traI, whose N- or C-termini either flanked or coincided with this region, were purified and assessed for catalytic activity. Amino acids 1-306 contain the transesterase activity while amino acids 309-1504 contain the helicase activity. The C-terminal 252 amino acids of the 1756 amino acid TraI protein are not required for either helicase or transesterase activity. Protein and nucleic acid sequence similarity searches indicate that the occurrence of both transesterase- and helicase-associated motifs in a conjugative DNA transfer initiator protein is rare. Only two examples (other than R100-TraI) were found; R388-TrwC and R46 (pKM101)-TraH, belonging respectively to the IncW and IncN group of broad host range conjugative plasmids. The most significant structural difference between these proteins and TraI is that TraI contains an additional region of approximately 650 residues between the transesterase domain and the helicase-associated motifs. This region is required for helicase activity.


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