Sites of covalent modification in Trg, a sensory transducer of Escherichia coli.
Open Access
- 1 May 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (13) , 6039-6045
- https://doi.org/10.1016/s0021-9258(18)45534-2
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Surface structure recognized for covalent modification of the aspartate receptor in chemotaxis.Proceedings of the National Academy of Sciences, 1986
- Chapter 1 Sensory Transduction in BacteriaPublished by Elsevier ,1985
- Structure of the Trg protein: Homologies with and differences from other sensory transducers of Escherichia coli.Proceedings of the National Academy of Sciences, 1984
- Separation of Signal Transduction and Adaptation Functions of the Aspartate Receptor in Bacterial SensingScience, 1983
- Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product.Proceedings of the National Academy of Sciences, 1983
- Sensory transducers of E. coli are composed of discrete structural and functional domainsCell, 1983
- Structure of the serine chemoreceptor in Escherichia coliNature, 1983
- Adaptation in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducer proteinsCell, 1982
- The methyl-accepting chemotaxis proteins of E. coli: A repellent-stimulated, covalent modification, distinct from methylationCell, 1981
- Multiple methylation of methyl-accepting chemotaxis proteins during adaptation of E. coli to chemical stimuliPublished by Elsevier ,1980