The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer.
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.
Sastre
J I
JI
Department of Molecular Biology, University of Cantabria, 39011 Santander, Spain.
Cabezón
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de la Cruz
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003227:Conjugation, Genetic; D004269:DNA, Bacterial; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D005144:F Factor; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D016296:Mutagenesis
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C064957:traD protein, E coli