The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer - PubMed (original) (raw)

The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer

J I Sastre et al. J Bacteriol. 1998 Nov.

Abstract

We isolated and characterized traD mutants with an altered specificity of interaction with relaxosomes of various conjugative (F and R388) and mobilizable (RSF1010 and ColE1) plasmids. The change in specificity was due to a loss of some amino acids in the carboxyl terminus of TraD that resulted in a broadening of the range of mobilizable relaxosomes at the expense of a decrease in the efficiency of F-plasmid transfer.

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Figures

FIG. 1

Comparison of TrwB with TraD and a series of TraD mutants in the carboxyl-terminal region. The upper part of the figure shows a schematic alignment of TrwB and TraD. Solid boxes represent predicted transmembrane segments, and shaded segments represent theoretical nucleoside triphosphate-binding motifs. When the amino acid sequences of TrwB and TraD were aligned, C-terminal residue 507 of TrwB aligned with residue 576 of TraD. The lower part of the figure shows the amino acid sequences of the carboxyl-terminal regions of TraD and its derivatives. The plasmids that encode each of the proteins are shown in parentheses. Superscript numbers correspond to the positions of the corresponding amino acids in the sequence of TraD. Amino acids that differ from those of TraD are underlined. Asterisks represent the ends of the proteins.

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