T J Su, M R Tock, S U Egelhaaf, W C Poon, and D T Dryden (2005)
Dna bending by m.ecoki methyltransferase is coupled to nucleotide flipping
Nucleic Acids Research 33:3235–3244.
The maintenance methyltransferase M.EcoKI recognizes the
bipartite DNA sequence 5'-A (A) under bar CNNN-NNNG (T) under
bar GC-3', where N is any nucleotide. M.EcoKI preferentially
methylates a sequence already containing a methylated adenine
at or complementary to the underlined bases in the sequence.
We find that the introduction of a single-stranded gap in the
middle of the non-specific spacer, of up to 4 nt in length,
does not reduce the binding affinity of M.EcoKI despite the
removal of non-sequence-specific contacts between the protein
and the DNA phosphate backbone. Surprisingly, binding
affinity is enhanced in a manner predicted by simple polymer
models of DNA flexibility. However, the activity of the
enzyme declines to zero once the single-stranded region
reaches 4 nt in length. This indicates that the recognition
of methylation of the DNA is communicated between the two