Li J, Li G, Weis R M
Department of Chemistry and Graduate Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Biochemistry. 1997 Sep 30;36(39):11851-7. doi: 10.1021/bi971510h.
Covalent modification of receptors is a widespread phenomenon in signal transduction. In the chemosensory system of Escherichia coli, the reversible methylation of certain glutamic acid residues in the cytoplasmic domain of receptor homodimers mediates adaptation to stimuli. Here we report that the serine receptor is methylated by an inter-dimer process. Methyltransferase bound to one subunit in a serine receptor homodimer was found to catalyze the addition of methyl groups to a receptor subunit in an adjacent dimer in the membrane. These results demonstrate a role for inter-dimer interactions in transmembrane signaling.
受体的共价修饰是信号转导中一种普遍存在的现象。在大肠杆菌的化学感应系统中，受体同型二聚体胞质结构域中某些谷氨酸残基的可逆甲基化介导了对刺激的适应性。在此，我们报道丝氨酸受体通过二聚体间过程发生甲基化。我们发现，结合在丝氨酸受体同型二聚体一个亚基上的甲基转移酶催化甲基基团添加到膜中相邻二聚体的受体亚基上。这些结果证明了二聚体间相互作用在跨膜信号传导中的作用。
