Mj. Shapiro et al., INTERACTIONS BETWEEN THE METHYLATION SITES OF THE ESCHERICHIA-COLI ASPARTATE RECEPTOR-MEDIATED BY THE METHYLTRANSFERASE, The Journal of biological chemistry, 270(2), 1995, pp. 751-755
Mutations made at and near the methylation sites of the Escherichia co
li aspartate receptor were found to affect the methylation rates of th
e remaining methylation sites. The results supported a model in which
the methyltransferase enzyme contacts a residue seven amino acids to t
he C terminus of a site being methylated. The presence of a negatively
charged residue at that position inhibits methylation, whereas a neut
ral residue has no effect. Methylation sites in the wild type receptor
may also influence the methylation of other sites which are 7 residue
s away through a physical contact with the methyltransferase.