Nucleic Acids Research, Vol 25, Issue 9 1694-1700, Copyright © 1997 by Oxford University Press
PH Thorpe, D Ternent and NE Murray
The type I restriction and modification (R-M) enzyme from Salmonella
enterica serovar kaduna ( Sty SKI) recognises the DNA sequence 5'-
CGAT(N)7GTTA, an unusual target for a type I R-M system in that it
comprises two tetranucleotide components. The amino target recognition
domain (TRD) of Sty SKI recognises 5'-CGAT and shows 36% amino acid
identity with the carboxy TRD of Eco R124I which recognises the
complementary, but degenerate, sequence 5'-RTCG. Current models predict
that the amino and carboxy TRDs of the specificity subunit are in inverted
orientations within a structure with 2-fold rotational symmetry. The
complementary target sequences recognised by the amino TRD of Sty SKI and
the carboxy TRD of Eco R124I are consistent with the predicted inverted
positions of the TRDs. Amino TRDs of similar amino acid sequence have been
shown to recognise the same nucleotide sequence. The similarity reported
here, the first example of one between amino and carboxy TRDs, while
consistent with a conserved mechanism of target recognition, offers
additional flexibility in the evolution of sequence specificity by
increasing the potential diversity of DNA targets for a given number of
TRDs. Sty SKI identifies the first member of the IB family in Salmonella
species.
ARTICLES
The specificity of sty SKI, a type I restriction enzyme, implies a structure with rotational symmetry
Institute of Cell and Molecular Biology, Darwin Building, Kings Buildings, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK.
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