title: Interactions between the methylation sites of the Escherichia coli aspartate receptor mediated by the methyltransferase.
abstract: Mutations made at and near the methylation sites of the Escherichia coli aspartate receptor were found to affect the methylation rates of the remaining methylation sites. The results supported a model in which the methyltransferase enzyme contacts a residue seven amino acids to the C terminus of a site being methylated. The presence of a negatively charged residue at that position inhibits methylation, whereas a neutral residue has no effect. Methylation sites in the wild type receptor may also influence the methylation of other sites which are 7 residues away through a physical contact with the methyltransferase.
authors: Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206.
authors: M J
authors: MJ
authors: Shapiro
authors: D
authors: D
authors: Panomitros
authors: D E
authors: DE
authors: Koshland
mesh_terms: D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D017459:Receptors, Amino Acid / Q000378:metabolism*
chemical_list: D017459:Receptors, Amino Acid; C031959:aspartic acid receptor; D001224:Aspartic Acid; D008780:Methyltransferases